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...
Main Authors: | , , , , , , , |
---|---|
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/ |
_version_ |
1611496492226314240 |