Document Detail


Studies on the region involved in the transport activity of Escherichia coli TolC by chimeric protein analysis.
MedLine Citation:
PMID:  17350794     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Gram-negative bacteria possess the outer membrane protein TolC which acts as an exit duct across the outer membrane. However, the region involved in the transport activity of TolC has remained unclear. We analyzed this region by creating chimeric TolCs. First, we expressed the genes for TolCs of Vibrio parahaemolyticus (vp-tolC) and Salmonella typhimurium (sal-tolC) in Escherichia coli. The levels of sequence identity in the mature region of VP-TolC/EC-TolC and Sal-TolC/EC-TolC with maximum matching are 43% and 90%, respectively. We found that the transport activity of VP-TolC was weak compared with that of TolC of E. coli (EC-TolC) although the transport activity of Sal-TolC was similar to that of EC-TolC. A comparison of the sequence of the three tolCs showed that the sequence around the periplasmic region covering Asn-188 to Lys-214 of EC-TolC is lowly identical to that of VP-TolC although the region of EC-TolC is almost identical to that of Sal-TolC. We think, therefore, that the region covering Asn-188 to Lys-214 of EC-TolC may have an important role to express its transport activity in E. coli. To examine the possibility, we divided the region of EC-TolC into three and exchanged the gene for each portion with that of vp-tolC. These mutant ec-tolCs were expressed in E. coli and the activity of each chimeric TolC was measured. The results showed that the portion covering Val-198 to Lys-214 of EC-TolC is deeply involved in the transport activity.
Authors:
Hiroyasu Yamanaka; Satoshi Tadokoro; Masaya Miyano; Eizo Takahashi; Hidetomo Kobayashi; Keinosuke Okamoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-02-08
Journal Detail:
Title:  Microbial pathogenesis     Volume:  42     ISSN:  0882-4010     ISO Abbreviation:  Microb. Pathog.     Publication Date:    2007 May-Jun
Date Detail:
Created Date:  2007-05-02     Completed Date:  2007-07-26     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8606191     Medline TA:  Microb Pathog     Country:  England    
Other Details:
Languages:  eng     Pagination:  184-92     Citation Subset:  IM    
Affiliation:
Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University, Hiro-Koshingai, Kure, Hiroshima 737-0112, Japan. h-yamana@ps.hirokoku-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Outer Membrane Proteins / chemistry,  genetics,  metabolism*
Bacterial Toxins / metabolism
Cloning, Molecular
Crystallography, X-Ray
Enterotoxins / metabolism,  secretion
Escherichia coli / genetics,  metabolism*,  physiology
Escherichia coli Proteins / chemistry,  genetics,  metabolism*
Membrane Transport Proteins / chemistry,  genetics,  metabolism*
Models, Molecular
Molecular Sequence Data
Mutant Chimeric Proteins / metabolism
Salmonella typhimurium / genetics
Sequence Alignment
Vibrio parahaemolyticus / genetics
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Bacterial Toxins; 0/Enterotoxins; 0/Escherichia coli Proteins; 0/Membrane Transport Proteins; 0/Mutant Chimeric Proteins; 0/heat stable toxin (E coli); 0/tolC protein, E coli

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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