Document Detail


Critical involvement of the E373-D434 region in the acid sensitivity of a NhaB-type Na(+)/H(+) antiporter from Vibrio alginolyticus.
MedLine Citation:
PMID:  22953996     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been well established that VaNhaB, a NhaB-type Na(+)/H(+) antiporter found in Vibrio alginolyticus, exhibits a striking acid sensitivity. However, the molecular basis of the pH-dependent regulatory mechanism of the antiport activity is yet to be investigated. In this study, we generated various chimeric proteins composed of VaNhaB and a pH insensitive ortholog found in Escherichia coli (EcNhaB) and analyzed the pH responses of their Na(+)/H(+) antiport activities to search for the key residues or domains that are involved in the pH sensitivity of VaNhaB. Our results revealed the significant importance of a stretch of amino acid residues within the loop 8-loop 9 regions (E373-D434) responsible for the acid sensitivity of VaNhaB, along with the possible involvement of other unidentified residues that are widely spread in the primary structure of VaNhaB. Moreover, we demonstrated that the E373-D434 region of VaNhaB was able to confer some degree of acid sensitivity on our pH insensitive chimeric antiporter that is mainly composed of EcNhaB except for seven amino acid substitutions at the N-terminal end. This result strongly suggested the possibility that the E373-D434 region is able to act, at least partially, as machinery that diminishes the activity of the NhaB-type antiporter at an acidic pH.
Authors:
Wakako Kiriyama; Tatsunosuke Nakamura; Masahiro Fukuhara; Toshio Yamaguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-20
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-02     Completed Date:  2012-12-10     Revised Date:  2013-04-25    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7766-74     Citation Subset:  IM    
Affiliation:
Department of Microbiology, Niigata University of Pharmacy and Applied Life Sciences, Niigata 956-8603, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*,  genetics,  metabolism*
Cloning, Molecular
Escherichia coli / chemistry,  genetics,  metabolism
Escherichia coli Proteins / chemistry,  genetics,  metabolism
Genes, Bacterial
Hydrogen-Ion Concentration
Molecular Sequence Data
Protein Structure, Tertiary
Sequence Alignment
Sodium-Hydrogen Antiporter / chemistry*,  genetics,  metabolism*
Vibrio alginolyticus / chemistry,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Sodium-Hydrogen Antiporter
Comments/Corrections
Erratum In:
Biochemistry. 2013 Mar 19;52(11):2007

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


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