Document Detail

A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation.
MedLine Citation:
PMID:  20923769     Owner:  NLM     Status:  MEDLINE    
Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp(1015) in the cap region as the most critical residue. Substitution at this position yielded a DegP-sensitive intermediate that is located at the periplasmic side of the OM. Further analysis revealed that Trp(1015) is most likely required for initiation of processive folding of the β-helix at the cell surface, which drives sequential translocation of the Hbp passenger across the OM.
Zora Soprova; Ana Sauri; Peter van Ulsen; Jeremy R H Tame; Tanneke den Blaauwen; Wouter S P Jong; Joen Luirink
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-10-05
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-11-29     Completed Date:  2010-12-30     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  38224-33     Citation Subset:  IM    
Department of Molecular Microbiology, Institute of Molecular Cell Biology, VU University, 1081 HV Amsterdam, The Netherlands.
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MeSH Terms
Endopeptidases / chemistry*,  genetics,  metabolism
Escherichia coli / enzymology*,  genetics
Escherichia coli Proteins / chemistry*,  genetics,  metabolism
Protein Folding*
Protein Structure, Secondary
Protein Structure, Tertiary
Reg. No./Substance:
0/Escherichia coli Proteins; EC 3.4.-/Endopeptidases; EC 3.4.99.-/hemoglobin protease Hbp

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