論文

査読有り
2006年6月

Carboxyl-terminal hydrophilic tail of a NhaP type Na+/H+ antiporter from cyanobacteria is involved in the apparent affinity for Na+ and pH sensitivity

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
  • R Waditee
  • ,
  • T Buaboocha
  • ,
  • M Kato
  • ,
  • T Hibino
  • ,
  • S Suzuki
  • ,
  • T Nakamura
  • ,
  • T Takabe

450
1
開始ページ
113
終了ページ
121
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.abb.2006.02.013
出版者・発行元
ELSEVIER SCIENCE INC

Little information is available on the C-terminal hydrophilic tails of prokaryotic Na+/H+ antiporters. To address functional properties of the C-terminal tail, truncation mutants in this domain were constructed. Truncation of C-terminal amino acid residues of NhaP1 type antiporter from Synechocystis PCC6803 (SynNhaP1) did not change the V-max values, but increased the K-m values for Na+ and Li+ about 3 to 15-fold. Truncation of C-terminal tail of a halotolerant cyanobacterium Aphanothece halophytica (ApNhaP1) significantly decreased the V-max although it did not alter the K values for Na+. The C-terminal part of SynNhaP1 was expressed in E. coli and purified as a 16kDa soluble protein. Addition of purified polypeptide to the membrane vesicles expressing the C-terminal truncated SynNhaP1 increased the exchange activities. Change of Glu519 and Glu521 to Lys in C-terminal tail altered the pH dependence of Na+/H+ and Li+/H+ exchange activities. These results indicate that the specific acidic amino acid residues at C-terminal domain play important roles for the K-m and the pH dependence of the exchange activity. (c) 2006 Elsevier Inc. All rights reserved.

Web of Science ® 被引用回数 : 10

リンク情報
DOI
https://doi.org/10.1016/j.abb.2006.02.013
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000238330900012&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/j.abb.2006.02.013
  • ISSN : 0003-9861
  • Web of Science ID : WOS:000238330900012

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