The putative Agrobacterium transcriptional activator-like virulence protein VirD5 may target T-complex to prevent the degradation of coat proteins in the plant cell nucleus

© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 203(2014), 4 vom: 20. Sept., Seite 1266-1281
1. Verfasser: Wang, Yafei (VerfasserIn)
Weitere Verfasser: Peng, Wei, Zhou, Xu, Huang, Fei, Shao, Lingyun, Luo, Meizhong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Agrobacterium AtVIP1 T-complex VBF VirD5 VirE2 coat proteins transcriptional activator-like virulence protein mehr... Arabidopsis Proteins Bacterial Proteins DNA, Bacterial T-DNA Trans-Activators VIP1 protein, Arabidopsis Virulence Factors alpha Karyopherins
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245 1 4 |a The putative Agrobacterium transcriptional activator-like virulence protein VirD5 may target T-complex to prevent the degradation of coat proteins in the plant cell nucleus 
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520 |a Agrobacterium exports at least five virulence proteins (VirE2, VirE3, VirF, VirD2, VirD5) into host cells and hijacks some host plant factors to facilitate its transformation process. Random DNA binding selection assays (RDSAs), electrophoretic mobility shift assays (EMSAs) and yeast one-hybrid systems were used to identify protein-bound DNA elements. Bimolecular fluorescence complementation, glutathione S-transferase pull-down and yeast two-hybrid assays were used to detect protein interactions. Protoplast transformation, coprecipitation, competitive binding and cell-free degradation assays were used to analyze the relationships among proteins. We found that Agrobacterium VirD5 exhibits transcriptional activation activity in yeast, is located in the plant cell nucleus, and forms homodimers. A specific VirD5-bound DNA element designated D5RE (VirD5 response element) was identified. VirD5 interacted directly with Arabidopsis VirE2 Interacting Protein 1 (AtVIP1). However, the ternary complex of VirD5-AtVIP1-VirE2 could be detected, whereas that of VirD5-AtVIP1-VBF (AtVIP1 Binding F-box protein) could not. We demonstrated that VirD5 competes with VBF for binding to AtVIP1 and stabilizes AtVIP1 and VirE2 in the cell-free degradation system. Our results indicated that VirD5 may act as both a transcriptional activator-like effector to regulate host gene expression and a protector preventing the coat proteins of the T-complex from being quickly degraded by the host's ubiquitin proteasome system (UPS) 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Agrobacterium 
650 4 |a AtVIP1 
650 4 |a T-complex 
650 4 |a VBF 
650 4 |a VirD5 
650 4 |a VirE2 
650 4 |a coat proteins 
650 4 |a transcriptional activator-like virulence protein 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Bacterial Proteins  |2 NLM 
650 7 |a DNA, Bacterial  |2 NLM 
650 7 |a T-DNA  |2 NLM 
650 7 |a Trans-Activators  |2 NLM 
650 7 |a VIP1 protein, Arabidopsis  |2 NLM 
650 7 |a Virulence Factors  |2 NLM 
650 7 |a alpha Karyopherins  |2 NLM 
700 1 |a Peng, Wei  |e verfasserin  |4 aut 
700 1 |a Zhou, Xu  |e verfasserin  |4 aut 
700 1 |a Huang, Fei  |e verfasserin  |4 aut 
700 1 |a Shao, Lingyun  |e verfasserin  |4 aut 
700 1 |a Luo, Meizhong  |e verfasserin  |4 aut 
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856 4 0 |u http://dx.doi.org/10.1111/nph.12866  |3 Volltext 
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