An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation

Bacterial conjugation is a form of type IV secretion that transports protein and DNA to recipient cells. Specific bacteriophage exploit the conjugative pili and cell envelope spanning protein machinery of these systems to invade bacterial cells. Infection by phage R17 requires F-like pili and coupli...

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Main Authors: Lang, Silvia, Kirchberger, Paul C, Gruber, Christian J, Redzej, Adam, Raffl, Sandra, Zellnig, Guenther, Zangger, Klaus, Zechner, Ellen L
Format: Online
Language:English
Published: Blackwell Publishing Ltd 2011
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245843/
id pubmed-3245843
recordtype oai_dc
spelling pubmed-32458432011-12-28 An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation Lang, Silvia Kirchberger, Paul C Gruber, Christian J Redzej, Adam Raffl, Sandra Zellnig, Guenther Zangger, Klaus Zechner, Ellen L Research Articles Bacterial conjugation is a form of type IV secretion that transports protein and DNA to recipient cells. Specific bacteriophage exploit the conjugative pili and cell envelope spanning protein machinery of these systems to invade bacterial cells. Infection by phage R17 requires F-like pili and coupling protein TraD, which gates the cytoplasmic entrance of the secretion channel. Here we investigate the role of TraD in R17 nucleoprotein uptake and find parallels to secretion mechanisms. The relaxosome of IncFII plasmid R1 is required. A ternary complex of plasmid oriT, TraD and a novel activation domain within the N-terminal 992 residues of TraI contributes a key mechanism involving relaxase-associated properties of TraI, protein interaction and the TraD ATPase. Helicase-associated activities of TraI are dispensable. These findings distinguish for the first time specific protein domains and complexes that process extracellular signals into distinct activation stages in the type IV initiation pathway. The study also provided insights into the evolutionary interplay of phage and the plasmids they exploit. Related plasmid F adapted to R17 independently of TraI. It follows that selection for phage resistance drives not only variation in TraA pilins but diversifies TraD and its binding partners in a plasmid-specific manner. Blackwell Publishing Ltd 2011-12 2011-11-08 /pmc/articles/PMC3245843/ /pubmed/22066957 http://dx.doi.org/10.1111/j.1365-2958.2011.07872.x Text en © 2011 Blackwell Publishing Ltd http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lang, Silvia
Kirchberger, Paul C
Gruber, Christian J
Redzej, Adam
Raffl, Sandra
Zellnig, Guenther
Zangger, Klaus
Zechner, Ellen L
spellingShingle Lang, Silvia
Kirchberger, Paul C
Gruber, Christian J
Redzej, Adam
Raffl, Sandra
Zellnig, Guenther
Zangger, Klaus
Zechner, Ellen L
An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
author_facet Lang, Silvia
Kirchberger, Paul C
Gruber, Christian J
Redzej, Adam
Raffl, Sandra
Zellnig, Guenther
Zangger, Klaus
Zechner, Ellen L
author_sort Lang, Silvia
title An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
title_short An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
title_full An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
title_fullStr An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
title_full_unstemmed An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
title_sort activation domain of plasmid r1 trai protein delineates stages of gene transfer initiation
description Bacterial conjugation is a form of type IV secretion that transports protein and DNA to recipient cells. Specific bacteriophage exploit the conjugative pili and cell envelope spanning protein machinery of these systems to invade bacterial cells. Infection by phage R17 requires F-like pili and coupling protein TraD, which gates the cytoplasmic entrance of the secretion channel. Here we investigate the role of TraD in R17 nucleoprotein uptake and find parallels to secretion mechanisms. The relaxosome of IncFII plasmid R1 is required. A ternary complex of plasmid oriT, TraD and a novel activation domain within the N-terminal 992 residues of TraI contributes a key mechanism involving relaxase-associated properties of TraI, protein interaction and the TraD ATPase. Helicase-associated activities of TraI are dispensable. These findings distinguish for the first time specific protein domains and complexes that process extracellular signals into distinct activation stages in the type IV initiation pathway. The study also provided insights into the evolutionary interplay of phage and the plasmids they exploit. Related plasmid F adapted to R17 independently of TraI. It follows that selection for phage resistance drives not only variation in TraA pilins but diversifies TraD and its binding partners in a plasmid-specific manner.
publisher Blackwell Publishing Ltd
publishDate 2011
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245843/
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