Kleine Goehre

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Kleine Goehre

Diese Seite werde ich nach und nach mit tollen Bildern von Projekten mit Kleine Göhre Design füllen. Ganz aktuelle Arbeiten findest du im Blog. Schau doch mal​. Als eine Göre (oder als ein Gör) bezeichnet man insbesondere in Norddeutschland und im Berliner Dialekt scherzhaft oder abwertend ein kleines, unartiges. Auf unserem Youtube Kanal findet ihr viele tolle Ideen, Tutorials und Hilfestellungen zum Thema Plotten und Basteln mit den Dateien von kleine göhre design.

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kleine göhre - freche kleidung so individuell wie ihr kind. Wir sind Plotter-Gö(h)ren - kleine göhre Design has members. Diese Gruppe wurde gegründet für alle, die die Plotterdateien von kleine göhr.e. Plotterdatei "Sprüche Schule" - kleine göhr.e design. Wir kennen es alle. Die Zeit vergeht wie im Flug. Plötzlich ist die Kindergartenzeit vorbei und eine neue.

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Kleine Goehre

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Häweker, S. Mersmann, T. Mentzel, T. Boller, M. Mansfield and S. Robatzek Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB.

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The Biotrophic Phase of Ustilago maydis : Novel Determinants for Compatibility. In: Genomics of Disease Gustafson P, ed. Brefort, L. Molina, G. Mendoza-Mendoza, O.

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Feldbrügge Pheromone-regulated target genes respond differentially to MAPK phosphorylation of transcription factor Prf1.

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König, C. Julius, S. Homann, H. Göringer and M. Feldbrügge Combining SELEX and yeast three-hybrid system for the in vivo selection and classification of RNA aptamers.

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Nature : Maurer, F. Kaffarnik, O. Ladendorf, A. Brachmann, J. Kämper, and M. Feldbrügge Tetracycline-regulated gene expression in the pathogen Ustilago maydis.

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In: The Mycota I: growth, differentiation and sexuality R. Kües, eds. Göhre, F. Ossenbühl, M. Eichacker and J.

Rochaix One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas.

Plant Cell 18 : Hu, B. Potthoff, C. Hollenberg and M. Ramezani-Rad Mdy2, a ubiquitin-like UBL -domain protein, is required for efficient mating in Saccharomyces cerevisiae.

J Cell Sci. Becht, E. Vollmeister, and M. Feldbrügge A role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis.

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Göhre, J. Meurer, A. Krieger-Liszkay, J. Rochaix and L. Eichacker Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3.

Plant Cell 16 : Müller, G. Weinzierl, A. Feldbrügge, and R. Kahmann Mating and pathogenic development of the smut fungus Ustilago maydis are regulated by one MAP kinase cascade.

Cell 2 : Kaffarnik, P. Leibundgut, R. Feldbrügge PKA and MAPK phosphorylation of Prf1 allows promoter discrimination in Ustilago maydis.

Ramezani-Rad, C. Hollenberg, J. Lauber, H. Wedler, E. Griess, C. Wagner, K. Albermann, J. Hani, M.

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Kessler, and M. Feldbrügge Structure-function analysis of lipopeptide pheromones from the plant pathogen Ustilago maydis.

Ramezani-Rad The role of adaptor protein Stedependent regulation of the MAPKKK Ste11 in multiple signalling pathways of yeast.

Genetics 43 : Bellafiore, P. Ferris, H. Naver, V. Göhre and J. Plant Cell 14 : La Fontaine, J. Quinn, S. Nakamoto, M. Page, V. Moseley, J.

Kropat and S. Merchant Copper-Dependent Iron Assimilation Pathway in the Model Photosynthetic Eukaryote Chlamydomonas reinhardtii.

Eukaryotic Cell 1 : Feldbrügge, P. Arizti, M. Sullivan, P. Zamore, J. Belasco and P. Green Comparative analysis of the plant mRNA-destabilizing element, DST, in mammalian and tobacco cells.

Plant Mol. Loubradou, A. Kahmann A homologue of the transcriptional repressor Ssn6p antagonizes cAMP signalling in Ustilago maydis.

Jansen, F. Bühring, C. Basse, P. Krüger, C. Aichinger, K. Hansson, A. Katzenberger, G. Leibbrandt, J. Torreblanca, M.

Kahmann Communication between Ustilago maydis and its host plant maize. In: IC-MPMI Congress Proceedings: Biology of Plant-Microbe Interactions Vol.

Bisseling, W. Stiekema, eds. Kahmann, G. Steinberg, C. Basse, M. Feldbrügge, and J. Kämper Ustilago maydis , the causative agent of corn smut disease.

In: Fungal Pathology J. Kronstad, ed. Kluwer Academic publishers, Dordrecht, pp. Krüger, G. Loubradou, G.

Wanner, E. Regenfelder, M. Kahmann Activation of the cAMP pathway in Ustilago maydis reduces fungal proliferation and teliospore formation in plant tumors.

Plant-Microbe Interact. Kahmann, C. Basse, and M. Feldbrügge Fungal-plant signalling in the Ustilago maydis -maize pathosystem.

Müller, C. Aichinger, M. Kahmann The MAP kinase kpp2 regulates mating and pathogenic development in Ustilago maydis. Entian, C.

Hollenberg, G. Jansen and M. Ramezani Rad et al. Ramezani Rad, G. Bühring and C. Hollenberg Ste50p is involved in regulating filamentous growth in the yeast Saccharomyces cerevisiae and associates with Ste11p.

Genetics : Sprenger, K. Hahlbrock, and B. Weisshaar PcMYB1, a novel plant protein containing a DNA-binding domain with one MYB repeat, interacts in vivo with a light-regulatory promoter unit.

Plant J. Weisshaar The transcriptional regulator CPRF1: expression analysis and gene structure. Dujon, M. Ramezani Rad, B. Habbig, U. Hattenhorst, C.

Hollenberg et al. Rad, B. Habbig, G. Jansen, U. Hattenhorst, M. Kroll and C. Hollenberg Analysis of the DNA sequence of a bp region on the left arm of yeast chromosome XV.

YEAST 13 : Xu, G. Thoma, C. Hollenberg, M. Ramezani Rad, M. Molecular Microbiology 20 : Galibert, M. Fritz, L. Kirchrath, C.

Jin, Y. Jang, M. Kim, M. Rad, L. Kirchrath, R. Seong, S. Hong, C. Hollenberg and S. Park Characterization of SFP2, a putative sulfate permease gene of Saccharomyces cerevisiae.

Rad, H. Phan, L. Kirchrath, P. Tan, T. Kirchhausen, C. Hollenberg and G. Cell Science : Sprenger, M. Dinkelbach, K. Yazaki, K. Harter, and B. Weisshaar Functional analysis of a light-responsive plant bZIP transcriptional regulator.

Plant Cell 6 : Feldmann, M. Ramezani Rad, L. Kirchrath, G. Xu, C. Ramezani Rad, C. Kirchrath and C. YEAST 10 : Ramezani Rad and H.

Katz Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum.

FEMS Microbiology Lett. Kawalleck, I. Somssich, M. Weisshaar Polyubiquitin gene expression and structural properties of the ubi gene in Petroselinum crispum.

Rad, G. Xu and C. Hollenberg STE50, a novel gene required for activation of conjugation at an early step of mating in Saccharomyces cerevisiae.

Oliver, Q. Agostoni-Carbone, M. Aigle, L. Alberghina, D. Alexandraki, G. Antoine, R. Anwar, J.

Ballesta, P. Benit, G. Berben, E. Bergantino, N. Biteau, P. Bolle, M. Bolotin-Fukuhara, A. Brown, A. Brown, J. Buhler, C.

Carcano, G. Carignani, H. Cederberg, R. Chanet, R. Contreras, M. Crouzet, B. Daignan-Fornier, E. Defoor, M. Delgado, J. Demolder, C. Doira, E.

Dubois, B. Dujon, A. Dusterhoft, D. Erdmann, M. Esteban, F. Fabre, C. Fairhead, G. Faye, H. Feldmann, W. Fiers, M. Francingues-Gaillard, L.

Given that AvrPto inhibits the autophosphorylation of FLS2 and EFR, it likely acts as a kinase inhibitor. This suggests that the observed interaction with BAK1 was specific for AvrPto.

It is possible that the observed lack of interaction between AvrPto and BAK1 was caused by differences in the experimental conditions. However, it cannot be excluded that the presence of the nYFP fusion partner interfered with the ability of AvrPto to dissociate the FLS2-BAK1 complex.

In addition to AvrPto, the distantly related effector AvrPtoB suppresses PTI responses Fig. AvrPtoB is presumably activated in planta by phosphorylation of the serine residue at position , suggesting that it mimics a substrate of a plant kinase Xiao, Giavalisco and Martin Given that the exchange of S to alanine leads to a loss of the virulence activity of AvrPtoB, phosphorylation of AvrPtoB is presumably required for protein function Xiao, Giavalisco and Martin The tyrosine phosphatase HopAO1 formerly known as HopPtoD2 from P.

Reduced phosphorylation of EFR presumably interferes with downstream signaling pathways which involve BAK1. It remains to be investigated whether HopAO1 suppresses EFR-mediated signaling by interfering with the phosphorylation of Y of EFR.

An additional effector from P. It is still unknown whether BAK1 is a substrate of the HopF2 ADP-RT activity. HopF2 presumably interferes with stomatal immunity independently of its ADP-RT activity because transgenic Arabidopsis plants expressing HopF2 or the catalytically inactive HopF2 DA derivative were impaired in stomatal closure upon treatment with P.

AvrPphB from P. AvrPphB also cleaves the kinase RIPK RPM1-induced protein kinase , which is required for the phosphorylation of the immune regulator RIN4 Russell, Ashfield and Innes see below.

AvrAC from X. In addition to BIK1, AvrAC interacts with and uridylates other RLCKs of the family VII, which is the largest family of RLCKs and includes several RLCKs involved in plant immune responses.

Uridylylation of PBL2 by AvrAC triggers ETI responses, which depend on the pseudokinase RKS1 and the R protein ZAR1 see below.

PRR-mediated immune responses often involve the activation of MAPK cascades. These signaling pathways are attractive targets for type III effectors because they contribute to various cellular pathways.

MAP3Ks are serine or threonine kinases and activate MAP2Ks also designated MEK via phosphorylation Rodriguez, Petersen and Mundy Among the well-studied MAPKs from plants are MPK3, MPK4 and MPK6, which are involved in defense responses.

MPK3 and MPK6 are part of a signaling cascade, which is activated by the MAP3K MEKK1 and the two MAP2Ks MKK4 and MKK5 Meng and Zhang Fig.

A second signaling cascade involves the MAP3K MEKK1, the two MAP2Ks MKK1 and MKK2 as well as MPK4 Meng and Zhang Influence of type III effectors on MAPK signaling pathways.

A Schematic overview on MAPK signaling pathways involved in plant defense responses. The activation of MAPKs directly or indirectly leads to the release of transcription factors TFs , which trigger the expression of defense genes.

Known substrates of MPK4 are MKS1, RIN4 and the MP3K MEKK2 also designated SUMM1. Phosphorylation of MKS1 by MPK4 leads to the release of the MKS1-bound TF WRKY33, which subsequently activates gene expression.

MPK4 also phosphorylates the MAP3K MEKK2 and presumably results in its inactivation. MPK4-mediated inactivation of MEKK2 leads to the suppression of ETI responses triggered by the CC-NB-LRR R protein SUMM2, which likely guards MEKK2 see the text for details.

B HopF2 from P. HopF2 also interacts with MPK6, yet, the outcome of this interaction is unknown. C The putative phosphothreonine lyase HopAI1 from P.

Furthermore, HopAI1 suppresses the kinase activity of MPK4 and thus the phosphorylation of the MPK4 substrates MKS1 and MEKK2. It has not yet been shown whether HopAI1 also interferes with the MPK4-mediated phosphorylation of RIN4 indicated by a dashed arrow and a questionmark.

The loss of MPK4 activity leads to the activation of MEKK2 indicated by a red asterisk , which in turn triggers SUMM2-mediated ETI see the text for details.

D AvrB from P. AvrB interacts with MPK4 and leads to its phosphorylation and thus activation. The efficient interaction between AvrB and MPK4 depends on RAR1, which presumably acts as a linker between AvrB and Hsp Hsp90 promotes the activity of MPK4 as is indicated by a red asterisk see the text for details.

Notably, MPK4 was initially identified as a negative regulator of plant immunity because mutations in MPK4 lead to the activation of defense responses Meng and Zhang Genetic screens for suppressor mutations in mkk1mkk2 plants led to the identification of SUMM1 and the R protein SUMM2.

Given the finding that overexpression of SUMM1 activates SUMM2-dependent defense responses, it was proposed that SUMM1 is negatively regulated by MPK4.

Effectors, which interfere with MAPK signaling pathways and SUMM2-mediated defense, include HopF2, HopAI1 and AvrB from P. As is detailed below, the ADP-RT HopF2 presumably inactivates the MP2K MKK5, whereas HopAI1 suppresses the activities of MAPKs.

AvrB, however, activates the MAPK MPK4, suggesting that effector proteins from P. The functions of HopF2, HopAI1 and AvrB are also summarized in Fig.

The ADP-RT HopF2 from P. An additional effector, which suppresses MAPK activities, is HopAI1 from P. The analysis of hopAI1- transgenic Arabidopsis plants revealed that HopAI1 suppresses the kinase activities of MPK3, MPK4 and MPK6 and thus interferes with plant defense responses, e.

In contrast to the HopAI1-mediated dephosphorylation and inactivation of MPK4, AvrB from P. Thus, HopAI1 and AvrB have opposing activities with regard to the phosphorylation of MPK4.

The eukaryotic 26S proteasome plays a central role in many cellular processes including hormone signaling and defense responses and is a virulence target of several type III effectors Price and Kwaik ; Dudler ; Duplan and Rivas ; Banfield The proteasome is composed of a 20S core particle and two 19S regulatory subunits, which recognize ubiquitinated proteins.

Ubiquitin is a highly conserved amino acid polypeptide and is often linked to other ubiquitin molecules via the lysine residue at position 48 Pickart Plants possess only one or two E1 proteins but a significantly higher number of E2 and E3 proteins e.

E3 ubiquitin ligases are single or multisubunit proteins, which interact with E2 enzymes via a HECT homologous to E6-associated protein C-terminus , a RING really interesting new gene or a U-box domain Chen and Hellmann Very well studied are SCF SKP1 [S-phase kinase-associated protein 1]-like-cullin 1-F-box complexes, which are multimeric RING-finger E3 ligases and play a central role in phytohormone signaling Shabek and Zheng SCF complexes consist of a cullin protein as a central scaffold, which associates via its C-terminal region with the RING protein RBX1 RING box 1.

The N-terminal part of the cullin protein is connected via a SKP1-like protein with a member of the F-box protein family, which provides the binding sites for the substrates of the SCF complex Vierstra ; Chen and Hellmann Fig.

F-box proteins contain the F-box motif, i. Contribution of type III effectors to proteasome-dependent protein degradation. A Model of the proteasome-dependent protein degradation pathway.

Ubiquitin Ub is activated by the ubiquitin-activating enzyme E1 and transferred to the ubiquitin-conjugating enzyme E2 , which interacts with the ubiquitin ligase E3.

E3 ubiquitin ligases are divided into several classes according to the presence of a HECT, RING or U-box domain. RING domain-containing E3 ubiquitin ligases can be part of a multimeric protein complex such as the SCF complex, which consists of a RING-box protein, the molecular scaffold protein cullin, an Arabidopsis SKP1-like protein ASK1 and an F-box protein, which binds the substrate of the E3 ligase.

E3 enzymes mediate the transfer of ubiquitin molecules to the substrate, thus leading to the formation of poly-ubiquitin chains, which allow the targeting of proteins to the proteasome.

The proteasome consists of two 19S regulatory and a 20S core particle and catalyzes the unfolding and degradation of polyubiquitinated proteins.

B Domain structure of the effector protein AvrPtoB from P. The regions of AvrPtoB, which provide binding sites for the AvrPtoB interaction partners Pto, Bti9, Fen, FLS2 and BAK1, are indicated.

Experimental evidence for the presence of two Pto-binding sites in AvrPtoB indicated as orange boxes was reported by Mathieu, Schwizer and Martin Numbers refer to amino acid positions in AvrPtoB.

C HopM1 from P. The HopM1-mediated degradation of AtMIN7 depends on the activity of the proteasome. D The effector protein XopL from X. XopL contains an N-terminal LRR and a C-terminal E3 ubiquitin ligase domain.

The plant targets of XopL are unknown. Numbers refer to amino acid positions in XopL. E GALA proteins from R. In agreement with this hypothesis, an interaction between GALA proteins and ASK proteins has been shown.

A contribution of GALA proteins to the ubiquitination of substrates of the SCF complex remains to be demonstrated. F XopJ from Xanthomonas spp.

XopJ leads to the degradation of RPT6. G XopP from X. Some effectors bind to E3 ligases or act themselves as E3 ligases and exploit the proteasome for the degradation of specific plant proteins.

Examples are AvrPtoB and HopM1 from P. Other effectors such as XopD from Xanthomonas spp. A similar effect is achieved by the bacterial tripeptide derivative syringolin, which is produced by several strains of P.

Furthermore, the effector XopP from Xanthomonas oryzae pv. The apparent contradictory activities of bacterial virulence factors, which suppress or promote the activity of the proteasome, might be caused by different spatial distributions of effectors in the plant cell or temporal differences in their synthesis or translocation.

The interference of single effector proteins with the proteasome and with proteasome-dependent protein degradation is summarized below and in Fig.

As mentioned above, AvrPtoB from P. An additional substrate of the E3 ubiquitin ligase activity of AvrPtoB is the kinase Fen, which is a member of the Pto resistance to P.

In the presence of AvrPtoB , however, which lacks the E3 ubiquitin ligase domain, Fen triggers defense responses in tomato. As is described below, Prf also detects full-length AvrPtoB and AvrPto and elicits ETI responses, which depend on the kinase Pto Oh and Martin In addition to its role in suppression of Fen-mediated defense responses, the C-terminal E3 ubiquitin ligase domain of AvrPtoB might also contribute to other virulence activities of AvrPtoB.

Furthermore, AvrPtoB failed to restore in planta growth of a P. Notably, a virulence function of the E3 ligase domain of AvrPtoB was not observed in additional studies, in which AvrPtoB and catalytically inactive AvrPtoB derivatives were shown to promote virulence of P.

The effector HopM1 from P. This is in agreement with the role of ARF-GEF proteins in vesicle trafficking. HopM1 leads to the destabilization of AtMIN7 when hopM1 and AtMIN7 are coexpressed in leaves of N.

The HopM1-mediated destabilization of AtMIN7 in N. Given the contribution of AtMIN7 to plant defense, HopM1 was suggested to suppress plant defense responses via degradation of AtMIN7.

HopM1 failed to trigger the degradation of AtMIN7 when delivered as heterologous protein by P. However, delivery of HopM1 by P. The type III effector XopL from X.

The analysis of different XopL protein regions revealed that the C-terminal E3 ubiquitin ligase domain is required for the XopL-mediated elicitation of plant cell death but dispensable for the suppression of PTI, which was observed in the presence of XopL.

GALA proteins also designated Rip [ Ralstonia protein injected into plant cells] G family from R. At least four GALA proteins from R.

However, it is yet unknown whether GALA proteins contribute to protein degradation. Notably, effector proteins with F-box motifs have also been identified as substrates of the type IV secretion systems from Agrobacterium tumefaciens and Legionella spp.

Price and Kwaik Several members of the YopJ family of putative proteases and acetyltransferases including XopJ from X. The analysis of fluorogenic peptide substrates revealed that the proteasome activity in N.

This suggests that the enzymatic activity of XopJ is required for the suppression of the proteasome. In agreement with the observed influence of XopJ on the proteasome, infection of pepper leaves with an X.

XopJ interacts with and degrades the ATPase RPT6 regulatory particle ATPase 6 of the 19S regulatory particle of the 26S proteasome at the plant plasma membrane Üstün, Bartetzko and Börnke ; Üstün and Börnke Fig.

It was, therefore, proposed that XopJ acts as a protease and interferes with the activity of the proteasome by targeting RPT6.

Similarly to XopJ, the homologous HopZ4 protein from P. Furthermore, the related effector protein AvrBsT from X. The effector protein XopP from X.

OsPUB44 presumably contributes to basal plant defense responses because rice OsPUB44 RNAi lines promote growth of X. XopP was, therefore, suggested to suppress plant defense by interfering with the activity of OsPUB Phytohormones are chemical messengers, which initiate signaling responses during various cellular processes such as plant growth, development, reproduction and responses to biotic and abiotic stress.

Phytohormones usually do not function independently of each other but are often controlled by a regulatory network, which links different hormone responses Robert-Seilaniantz, Grant and Jones ; Gimenez-Ibanez and Solano Signaling by several hormones such as auxin, jasmonic acid JA , ethylene ET and salicylic acid SA involves the proteasomal degradation of transcriptional repressors and the release or activation of transcription factors, which lead to hormone-induced gene expression.

Research in the model plant Arabidopsis revealed that JA, SA and ET are key players in plant defense against microbial pathogens.

While SA is usually involved in resistance against biotrophic and hemibiotrophic pathogens, JA and ET can act antagonistically to SA and promote resistance against necrotrophic pathogens Glazebrook Fig.

Due to the antagonistic interplay between JA and SA, the activation of JA-dependent defense responses often represses SA-induced signaling pathways, which are usually mounted upon infection by biotrophic pathogens Gimenez-Ibanez and Solano ; Kazan and Lyons In addition to JA, SA and ET, recent studies revealed a role of other phytohormones including auxin, cytokinins, brassinosteroids, abscisic acid and gibberellins in plant—pathogen interactions Gimenez-Ibanez and Solano ; Kazan and Lyons Interference of type III effectors with SA and JA signaling pathways.

SA-dependent defense responses are required for plant resistance against biotrophic pathogens whereas JA-dependent defense is mounted against necrotrophic pathogens.

SA and JA pathways thus act antagonistically and can suppress each other. Type III effectors from biotrophic or hemibiotrophic pathogens activate JA signaling pathways and suppress SA-mediated defense by the actions of translocated type III effectors.

SA-dependent defense responses depend on NPR1 non-expressor of PR genes , which is present in an oligomeric inactive state in the absence of SA.

Upon binding of SA, monomeric NPR1 binds to and activates transcription factors TF and thus induces the expression of SA-dependent genes Gimenez-Ibanez and Solano The effectors HopD1 and HopI1 from P.

The turnover of NPR1 is required for the expression of SA-responsive genes. Stabilization of NPR1, therefore, suppresses SA signaling Robert-Seilaniantz, Grant and Jones JA signaling pathways involve JAZ proteins and the SCF complex.

The bacterial toxin coronatine and the effector proteins AvrB, HopX1 and HopZ1 from P. Plant-pathogenic bacteria produce phytohormone mimics to interfere with hormone signaling pathways.

One prominent example is the phytotoxin coronatine, which is synthesized by a few pathovars of P. In addition to phytohormone mimics, plant-pathogenic bacteria deliver type III effector proteins to interfere with hormone signaling pathways.

Effectors, which interfere with JA signaling pathways, include the cysteine protease HopX1, the acetyltransferase HopZ1a and AvrB from P.

Furthermore, the cysteine protease AvrRpt2 from P. The functions of HopX1, HopZ1a, AvrB, AvrRpt2 and XopD are desribed below and summarized in Figs 5 and 6.

Modulation of JA, auxin and GA signaling pathways by type III effectors. A HopX1, HopZ1a and AvrB from P. Bioactive JA-Ile promotes the interaction between JAZ proteins and the F-box protein COI1, which is a component of the SCF complex.

The subsequent degradation of JAZ proteins leads to the release of JAZ-interacting transcription factors e. MYC2 , which activate the expression of JA-responsive genes.

The cysteine protease HopX1 directly or indirectly degrades several JAZ proteins independently of the JA receptor COI1 and thus activates the expression of JA-responsive genes.

The acetyltransferase HopZ1a acetylates JAZ proteins and leads to their proteasome-dependent degradation. The effector protein AvrB from P.

The interaction of AvrB with the RIN4-AHA1 complex promotes the interaction between JAZ proteins and COI1 and leads to the activation of JA-responsive genes.

B Auxin signaling pathways are targeted by the cysteine protease AvrRpt2 from P. ARFs subsequently activate the expression of auxin-responsive genes.

C XopD from X. GA-dependent signaling is controlled by DELLA proteins, which inactivate PIF phytochrome interacting factors transcription factors.

Binding of GA to its receptor GID1 leads to a conformational change in GID1, which subsequently binds to DELLA proteins.

The formation of a GID1-DELLA complex promotes the interaction between DELLA proteins and the F-box protein SLY and thus the proteasome-dependent degradation of DELLA proteins.

This leads to the release of PIF transcription factors, which activate the expression of GA-responsive genes. XopD Xcc presumably interferes with the binding of GID1 to DELLA proteins and delays the GA-induced degradation of the DELLA protein RGA.

Notably, however, an influence of XopD Xcc on the transcription of GA-responsive genes has not yet been detected. HopX1 and HopZ1a from P.

JAZ proteins act as transcriptional repressors and interact with and inhibit transcription factors. JAZ proteins are degraded by the proteasome in the presence of JA-Ile, which is perceived by the JA receptor and F-box protein COI1 coronatine insensitive 1.

This leads to the release of JAZ-interacting transcription factors and thus to the activation of JA-responsive gene expression Robert-Seilaniantz, Grant and Jones Fig.

The effector protein HopX1 is a cysteine protease and is delivered by P. Transient coexpression studies in N.

The HopX1-mediated degradation of JAZ proteins occurs independently of the JA receptor COI1 and leads to the activation of JA-responsive genes as well as to the repression of SA-induced signaling pathways.

JAZ proteins are also targeted by HopZ1a from P. HopZ1a leads to the degradation of JAZ proteins and the induction of JA-responsive genes in Arabidopsis when delivered by a coronatine-deficient mutant derivative of P.

It remains to be investigated whether the acetylation of JAZ proteins by HopZ1a facilitates their COI1-dependent degradation. The type III effector AvrB from P.

Increased concentrations of charged solutes in the guard cells result in a water uptake and elevated turgor, thus leading to stomatal opening.

RIN4 also interacts with AHA1 and promotes its activity Liu, Elmore and Coaker see below. Transient expression studies in N.

The biochemical mechanism underlying the AvrB-RIN4-AHA1-mediated induction of COI1-JAZ interactions is yet unknown. The cysteine protease AvrRpt2 from P.

Members of the XopD family of nuclear-localized effector proteins from Xanthomonas spp. Sequence comparisons revealed variations in the domain organization of XopD family members.

While XopD from X. XopD Xcv deSUMOylates and thus destabilizes SlERF4 from Solanum lycopersicum Kim, Stork and Mudgett As the presence of proteasome inhibitor interferes with the XopD-induced destabilization of SlERF4, it was suggested that XopD facilitates the degradation of SlERF4 by the proteasome Kim, Stork and Mudgett SlERF4 is presumably involved in the regulation of ET biosynthesis and colocalizes with XopD to subnuclear foci Kim, Stork and Mudgett In agreement with the observed XopD-mediated destabilization of SlERF4, XopD Xcv leads to reduced ET levels in infected plant tissue and suppresses the expression of genes involved in ET production Kim, Stork and Mudgett Given that ET production is required for plant immunity, XopD Xcv likely deSUMOylates SlERF4 to suppress plant defense responses Kim, Stork and Mudgett Interference of type III effector proteins with plant gene expression.

A Domain organization of XopD proteins from Xanthomonas spp. XopD family members consist of a C-terminal cysteine protease domain and N-terminal EAR motifs.

Additionally, XopD from X. XopD Xcc was shown to interact with and stabilize DELLA proteins via the EAR motif-containing region. Furthermore, XopD Xcc interacts with and deSUMOylates the transcription factor HFR1.

XopD XccB and XopD Xcv bind to the transcription factor MYB30 via the HLH domain and suppress its transcriptional activity.

XopD Xcv deSUMOylates and thus destabilizes the transcription factor ERF4. Numbers refer to amino acid positions in XopD Xcv B Domain organization and DNA-binding specificity of the TAL effector Hax homolog of AvrBs3 in Xanthomonas 3 from X.

TAL effectors contain a C-terminal acidic activation domain AAD , two NLSs and a central protein region with repeats.

The RVDs of Hax3 and the matching bases in the EBE in the promoter regions of Hax3-induced genes are indicated.

C Domain organization of HsvG from P. HsvG contains N- and C-terminal NLSs, an N-terminal HTH region and two repeats of 71 and 74 amino acids R1 and R2 , which confer transcription activation activity in yeast.

The repeats determine the specificity of plant gene activation indicated by a white arrow but are dispensable for DNA binding of HsvG, which depends on the N-terminal region.

Numbers refer to amino acid positions in HsvG. D Modification of RRS1-R by the effector protein PopP2 from R. The TIR-NB-LRR protein RRS1-R forms a dimer and binds via its WRKY domain to a DNA motif W box present in promoters of target genes of WRKY transcription factors.

PopP2 interacts with and acetylates the WRKY domain of RRS1-R and thus interferes with its DNA binding.

The additional PopP2 interaction partner RD19, which is a predicted protease, is presumably not acetylated by PopP2.

RRS1-R also interacts with the R protein RPS4, which is required for the induction of ETI and is not shown in this figure see the text for details.

E The mono-ADP-RT HopU1 from P. GRP7 also interacts with the PRRs FLS2 and EFR and with FLS2 and EFR transcripts, and was, therefore, assumed to promote PRR translation.

ADP-ribosylation of GRP7 by HopU1 reduces the ability of GRP7 to bind to RNA and might suppress FLS2 and EFR protein synthesis.

F HopD1 from P. Furthermore, HopD1 suppresses ETI responses. The mechanisms underlying the HopD1-mediated inhibition of NTL9-dependent gene expression are unknown.

DELLA proteins are negative regulators of GA response activators and colocalize with XopD Xcc to the plant nucleus. The degradation of DELLA proteins by the proteasome is stimulated in the presence of GA, which binds to its receptor GID1 gibberellin insensitive dwarf 1 Hauvermale, Ariizumi and Steber GA promotes the interaction between GID1 and DELLA proteins, which are subsequently targeted to the F-box protein SLY and degraded by the proteasome.

The degradation of DELLA proteins leads to the activation of GA response activators, which induce the expression of GA-responsive genes Hauvermale, Ariizumi and Steber Fig.

One effective strategy employed by type III effectors to interfere with plant cellular processes is the manipulation of gene expression on the transcriptional or posttranscriptional level.

Effector proteins, which are directly imported into the nucleus and either bind to DNA or to components of the plant transcription machinery, are transcription activator-like TAL effectors from Xanthomonas spp.

Type III effectors, which target plant transcription factors and RNA-binding proteins, include XopD proteins from Xanthomonas spp.

Known mechanisms underlying type III effector-mediated modulation of plant gene expression are summarized below and in Fig. Members of the TAL effector family were mainly isolated from Xanthomonas spp.

However, related proteins are also present in R. Characteristic features of TAL effectors include a C-terminal acidic activation domain and nuclear localization signals NLSs , which are required for the import of TAL effectors into the plant nucleus Boch and Bonas DNA binding is mediated by the central region of TAL effectors, which consists of 1.

A minimum of 6. The repeats are nearly amino acid sequence identical and usually 33 to 35 amino acids long, but longer and shorter repeats have also been described Boch and Bonas Sequence-specific binding to DNA bases depends on the polymorphic amino acids at positions 12 and 13 of each repeat of the TAL effector.

The RVDs determine the binding specificity of TAL effectors to DNA. In the past years, numerous studies have focused on the analysis of the binding specificity of TAL effectors to the effector-binding elements EBEs in the promoter regions of plant target genes.

Repeat number and RVDs determine the number and nature of DNA bases, which are bound by the TAL effectors. Replacement of the natural RVDs of specific repeats by all possible RVD combinations revealed that not all artificial RVDs are functional.

In addition to the RVD composition, the length of the repeats affects the binding to DNA bases. The looping-out of repeats allows a shift of the following repeats by one nucleotide position in the EBE.

The groundbreaking discovery of the TAL-DNA-binding code has marked the beginning of a new era in genome engineering because it has led to the design of various genome editing tools e.

TAL effector nucleases , which allow sequence-specific binding of DNA-modifying enzymes by the use of TAL effector repeats as fusion partners Scharenberg, Duchateau and Smith ; Mahfouz, Piatek and Stewart The mechanisms leading to transcriptional activation of plant genes by TAL effectors are not yet understood.

It is, therefore, assumed that TAL effectors do not only bind to DNA but also associate with components of the plant transcription machinery to activate gene expression.

Among the plant genes targeted by TAL effectors are those encoding transcription factors and proteins involved in senescence, development, stress response and sugar transport Table S2, Supporting Information.

Examples are the SWEET genes from rice, which are involved in sucrose or fructose transport and are induced by TAL effectors from the systemic rice pathogen X.

TAL target genes, which contribute to virulence, are also referred to as plant susceptibility genes. Notably, however, TAL effectors can also induce the expression of plant resistance R genes and thus trigger ETI responses Boch, Bonas and Lahaye TAL effector-responsive R genes have been categorized into different groups including recessive and dominant R genes.

In this case, resistance is the result of the loss of induction of an S gene. The third group of TAL effector-responsive R genes are executor R genes, which contain EBEs in their promoter regions and are specifically activated by matching TAL effectors Zhang, Yin and White Examples are Bs3 from pepper, and Xa10 , Xa23 and Xa27 from rice Table S2.

The engineering of executor R gene promoters allows gene induction by various TAL effectors and might help to improve strategies for plant resistance and disease control Boch, Bonas and Lahaye DNA binding has also been described for the effector protein HsvG, which is an important pathogenicity factor of the gall-forming plant-pathogenic bacterium P.

HsvG is homologous to the type III effector HsvB, which is required for pathogenicity of Pa. The results of yeast one-hybrid assays suggest that HsvG acts as a transcriptional activator.

These findings suggest that the repeats and not the DNA-binding region of HsvG and HsvB determine the specificity in target gene activation. Among the nuclear localized effectors, which presumably interfere with plant gene expression, are members of the XopD family from Xanthomonas spp.

As described above, XopD family members interfere with hormone signaling and cleave SUMO from SUMOylated proteins. It was, therefore, suggested that XopD family members suppress plant defense responses by targeting MYB Another effector protein, which modulates plant gene expression, is the YopJ family member and acetyltransferase PopP2 from R.

Notably, PopP2 does not only acetylate but also stabilizes RRS1-R. Type III effectors from plant-pathogenic bacteria do not only bind to DNA or transcription factors but can also interact with RNA-binding proteins.

One example is the mADP-RT HopU1 from P. Taken together, these findings suggest that HopU1 suppresses the GRP7-induced accumulation of FLS2 by ADP-ribosylation of GRP7.

HopD1 from P. NTL9 is a member of the NTLM1 NAC with transmembrane motif 1 family of transcription factors. This family is one of the largest families of plant transcription factors and is involved in various processes including developmental and stress-related signaling Nuruzzaman, Sharoni and Kikuchi SA is involved in various cellular processes including plant stomatal immunity, i.

Stomatal immunity is abolished in Arabidopsis ntl9 mutant plants and this phenotype is suppressed upon application of SA. Expression of NTL9-induced genes during ETI is reduced in the presence of HopD1.

As mentioned above, HopM1 from P. Taken together, these results suggest that HopM1 targets a protein to interfere with the activity of a transcriptional repressor.

The analysis of actin filaments using a GFP green fluorescent protein -fABD2 filamentous actin-binding domain 2 reporter fusion in Arabidopsis epidermis cells revealed a transient increase in actin filaments upon infection with Pseudomonas syringae pv.

A similar formation of actin filaments was observed upon treatment of plants with PAMPs and was shown to depend on FLS2, BAK1 and BIK1.

Twenty-four hours after infection with the P. No changes were induced by P. Infiltration of latrunculin B, which inhibits actin polymerization, promotes susceptibility of Arabidopsis leaves to bacterial infections and leads to an increased growth of P.

Influence of type III effectors on actin filaments and microtubules. A Infection of Arabidopsis cells with P. The infection with wild-type or T3S mutant strains leads to an increase in actin filaments 6 hours post infection.

Twenty-four hours post infection, the wild-type strain induces the formation of actin bundles and leads to a reduced number of actin filaments.

Actin filaments and bundles are indicated as yellow dashes. Aside from various songs which were used in the film, the soundtrack also includes parts of the film's score by Beckmann and Djorkaeff.

Bora Dagtekin announced in , that in a second movie will be released. On 7 September the film premiered in Munich.

On 2 September , the Mexican remake named No manches Frida El maestro suplente was released. From Wikipedia, the free encyclopedia. Theatrical release poster.

Constantin Film Rat Pack Filmproduktion. Release date. Running time. Various Artists. Main articles: Fack ju Göhte 2 and Fack ju Göhte 3.

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Buch erstellen Als PDF herunterladen Druckversion. Franz-Wachtel, B. The effector proteins AvrRpm1 and AvrB from P. Jankowski, K. C Model of the role of RIN4 during PTI. A Domain organization of RIN4 and list of known plant Ficken Mit äLteren Frauen partners of RIN4. On 7 September the film premiered in Munich. Feldbrügge Inside-Out: from endosomes to extracellular vesicles in fungal RNA transport. In: Genomics of Disease Gustafson P, ed. Disruption of the complex between EDS1 and RPS4 f. S-Adenosyl-L-methionine-dependent methyltransferases SAM-MT1 and SAM-MT2 Arabidopsis. Biochemical evidence for this hypothesis is still missing. Feldbrügge mRNA trafficking in fungi.

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