The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding

Zhida Zheng; Dejian Ma; Timothy L Yahr; Lingling Chen

doi:10.1016/j.bbrc.2011.11.070

Back

The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding

Journal article

Open access

Peer reviewed

The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding

Zhida Zheng, Dejian Ma, Timothy L Yahr and Lingling Chen

Biochemical and biophysical research communications, Vol.417(1), pp.129-134

01/06/2012

DOI: 10.1016/j.bbrc.2011.11.070

PMCID: PMC4930836

PMID: 22138394

Files and links (1)

url

http://doi.org/10.1016/j.bbrc.2011.11.070View

Open Access

Abstract

► Regulation of type III secretion system is mediated by secretion of ExsE. ► ExsE is globally unfolded and highly dynamic by NMR studies. ► The extended conformation of ExsE is important for its function. ► ExsE samples through conformations with localized structurally ordered regions. ► The transiently ordered elements may promote ExsE binding to the secretion chaperone. Many Gram-negative bacteria utilize a type III secretion system (T3SS) to deliver protein effectors to target host cells. Transcriptional control of T3SS gene expression is generally coupled to secretion through the release of a regulatory protein. T3SS gene expression in Pseudomonas aeruginosa is regulated by extracellular secretion of ExsE. ExsE is a small 81 residue protein that appears to lack a stable structural core as indicated by previous studies. In this study, we employed various NMR methods to characterize the structure of ExsE alone and when bound to its secretion chaperone ExsC. We found that ExsE is largely unfolded throughout the polypeptide chain, belonging to a class of proteins that are intrinsically disordered. The unfolded, extended conformation of ExsE may expedite efficient secretion through the narrow path of the T3SS secretion channel to activate gene expression in a timely manner. We also found that the structurally flexible ExsE samples through conformations with localized structurally ordered regions. Importantly, these transiently ordered elements are related to the secondary structures involved in binding ExsC based on a prior crystal structure of the ExsC–ExsE complex. These findings support the notion that preexisting structured elements facilitate binding of intrinsically disordered proteins to their targets.

The ExsE–ExsC interaction

T3SS substrate

Dynamics of ExsE

Intrinsically disordered proteins

NMR studies

Details

Title: Subtitle: The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding
Creators: Zhida Zheng - Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA
Dejian Ma - Department of Chemistry, Indiana University, Bloomington, IN 47405, USA
Timothy L Yahr - Department of Microbiology, University of Iowa, Iowa City, IA 52242, USA
Lingling Chen - Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA
Resource Type: Journal article
Publication Details: Biochemical and biophysical research communications, Vol.417(1), pp.129-134
DOI: 10.1016/j.bbrc.2011.11.070
PMID: 22138394
PMCID: PMC4930836
NLM abbreviation: Biochem Biophys Res Commun
ISSN: 0006-291X
eISSN: 1090-2104
Publisher: Elsevier Inc
Language: English
Date published: 01/06/2012
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001218702771

Metrics

25 Record Views

9 Times Cited - Web of Science