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Title: Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima

Abstract

Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930395
Report Number(s):
BNL-81117-2008-JA
Journal ID: ISSN 0907-4449; TRN: US200904%%675
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica Section D: Biological Crystallography; Journal Volume: D63
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BACTERIA; CROSS-LINKING; CRYSTALLOGRAPHY; ESCHERICHIA COLI; PROTEINS; RIBOSOMES; national synchrotron light source

Citation Formats

Martinez-Hackert,E., and Hendrickson, W. Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima. United States: N. p., 2007. Web. doi:10.1107/S090744490700964X.
Martinez-Hackert,E., & Hendrickson, W. Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima. United States. doi:10.1107/S090744490700964X.
Martinez-Hackert,E., and Hendrickson, W. Mon . "Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima". United States. doi:10.1107/S090744490700964X.
@article{osti_930395,
title = {Structures of and Interactions Between Domains of Trigger Factor from Thermotoga maritima},
author = {Martinez-Hackert,E. and Hendrickson, W.},
abstractNote = {Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces.},
doi = {10.1107/S090744490700964X},
journal = {Acta Crystallographica Section D: Biological Crystallography},
number = ,
volume = D63,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}