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Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens

Agrobacterium tumefaciens is a Gram-negative plant-pathogenic bacterium that causes crown gall disease by transferring and integrating its transferred DNA (T-DNA) into the host genome. We characterized the chromosomally encoded alpha-crystallin-type small heat-shock protein (α-Hsp) HspL, which was i...

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Autores principales: Tsai, Yun-Long, Wang, Ming-Hsuan, Gao, Chan, Klüsener, Sonja, Baron, Christian, Narberhaus, Franz, Lai, Erh-Min
Formato: Texto
Lenguaje:English
Publicado: Microbiology Society 2009
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885654/
https://www.ncbi.nlm.nih.gov/pubmed/19556291
http://dx.doi.org/10.1099/mic.0.030676-0
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author Tsai, Yun-Long
Wang, Ming-Hsuan
Gao, Chan
Klüsener, Sonja
Baron, Christian
Narberhaus, Franz
Lai, Erh-Min
author_facet Tsai, Yun-Long
Wang, Ming-Hsuan
Gao, Chan
Klüsener, Sonja
Baron, Christian
Narberhaus, Franz
Lai, Erh-Min
author_sort Tsai, Yun-Long
collection PubMed
description Agrobacterium tumefaciens is a Gram-negative plant-pathogenic bacterium that causes crown gall disease by transferring and integrating its transferred DNA (T-DNA) into the host genome. We characterized the chromosomally encoded alpha-crystallin-type small heat-shock protein (α-Hsp) HspL, which was induced by the virulence (vir) gene inducer acetosyringone (AS). The transcription of hspL but not three other α-Hsp genes (hspC, hspAT1, hspAT2) was upregulated by AS. Further expression analysis in various vir mutants suggested that AS-induced hspL transcription is not directly activated by the VirG response regulator but rather depends on the expression of VirG-activated virB genes encoding components of the type IV secretion system (T4SS). Among the 11 virB genes encoded by the virB operon, HspL protein levels were reduced in strains with deletions of virB6, virB8 or virB11. VirB protein accumulation but not virB transcription levels were reduced in an hspL deletion mutant early after AS induction, implying that HspL may affect the stability of individual VirB proteins or of the T4S complex directly or indirectly. Tumorigenesis efficiency and the VirB/D4-mediated conjugal transfer of an IncQ plasmid RSF1010 derivative between A. tumefaciens strains were reduced in the absence of HspL. In conclusion, increased HspL abundance is triggered in response to certain VirB protein(s) and plays a role in optimal VirB protein accumulation, VirB/D4-mediated DNA transfer and tumorigenesis.
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spelling pubmed-28856542010-07-06 Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens Tsai, Yun-Long Wang, Ming-Hsuan Gao, Chan Klüsener, Sonja Baron, Christian Narberhaus, Franz Lai, Erh-Min Microbiology (Reading) Microbial Pathogenicity Agrobacterium tumefaciens is a Gram-negative plant-pathogenic bacterium that causes crown gall disease by transferring and integrating its transferred DNA (T-DNA) into the host genome. We characterized the chromosomally encoded alpha-crystallin-type small heat-shock protein (α-Hsp) HspL, which was induced by the virulence (vir) gene inducer acetosyringone (AS). The transcription of hspL but not three other α-Hsp genes (hspC, hspAT1, hspAT2) was upregulated by AS. Further expression analysis in various vir mutants suggested that AS-induced hspL transcription is not directly activated by the VirG response regulator but rather depends on the expression of VirG-activated virB genes encoding components of the type IV secretion system (T4SS). Among the 11 virB genes encoded by the virB operon, HspL protein levels were reduced in strains with deletions of virB6, virB8 or virB11. VirB protein accumulation but not virB transcription levels were reduced in an hspL deletion mutant early after AS induction, implying that HspL may affect the stability of individual VirB proteins or of the T4S complex directly or indirectly. Tumorigenesis efficiency and the VirB/D4-mediated conjugal transfer of an IncQ plasmid RSF1010 derivative between A. tumefaciens strains were reduced in the absence of HspL. In conclusion, increased HspL abundance is triggered in response to certain VirB protein(s) and plays a role in optimal VirB protein accumulation, VirB/D4-mediated DNA transfer and tumorigenesis. Microbiology Society 2009-10 /pmc/articles/PMC2885654/ /pubmed/19556291 http://dx.doi.org/10.1099/mic.0.030676-0 Text en Copyright © 2009, SGM http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Microbial Pathogenicity
Tsai, Yun-Long
Wang, Ming-Hsuan
Gao, Chan
Klüsener, Sonja
Baron, Christian
Narberhaus, Franz
Lai, Erh-Min
Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title_full Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title_fullStr Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title_full_unstemmed Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title_short Small heat-shock protein HspL is induced by VirB protein(s) and promotes VirB/D4-mediated DNA transfer in Agrobacterium tumefaciens
title_sort small heat-shock protein hspl is induced by virb protein(s) and promotes virb/d4-mediated dna transfer in agrobacterium tumefaciens
topic Microbial Pathogenicity
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885654/
https://www.ncbi.nlm.nih.gov/pubmed/19556291
http://dx.doi.org/10.1099/mic.0.030676-0
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