Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Mitsui, K.
Right arrow Articles by Kanazawa, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mitsui, K.
Right arrow Articles by Kanazawa, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 2004, Vol. 135, No. 1 139-148
© 2004 The Japanese Biochemical Society

CELL

A Conserved Domain in the Tail Region of the Saccharomyces cerevisiae Na+/H+ Antiporter (Nha1p) Plays Important Roles in Localization and Salinity-Resistant Cell-Growth

Keiji Mitsui, Shinya Kamauchi, Norihiro Nakamura, Hiroki Inoue and Hiroshi Kanazawa*

Department of Biological Sciences, Graduate School of Science, Osaka University, 1-16 Machikaneyama-cho, Toyonaka City, Osaka 560-0043

The Saccharomyces cerevisiae Na+/H+ antiporter Nha1p has a two-domain structure consisting of an N-terminal integral membrane region and a C-terminal cytoplasmic region. We previously identified six distinct cytoplasmic domains (C1–C6) conserved among yeast species and here we performed detailed structure-function analysis of the C1 domain (16 residues). Deletion of the C1 domain causes extensive inhibition of cell-growth under high salinity conditions. Mutants with single residue deletions or various amino acid substitutions affecting the C1 domain were analyzed with respect to salinity-dependent growth and Nha1p localization. The C1 domain was found to consist of two subdomains: (i) The first three N-proximal residues, which in conjunction with the integral membrane region play a crucial role in the targeting of Nha1p to the cytoplasmic membrane, and (ii) the portion between Leu-439 and Thr-449, which is not required for localization, but in which four residues (Gly-440, Arg-441, His-442, and Ile-446) affect salinity-sensitive cell-growth by possibly influencing the antiporter activity. Based on the overall similarity of the two-domain structure of Nha1p to that of mammalian Na+/H+ antiporters, the functional importance of domains proximal to the membrane region is discussed.

* To whom correspondence should be addressed. E-mail: kanazawa{at}bio.sci.osaka-u.ac.jp


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
K. Mitsui, K. Hatakeyama, M. Matsushita, and H. Kanazawa
Saccharomyces cerevisiae Na+/H+ Antiporter Nha1p Associates with Lipid Rafts and Requires Sphingolipid for Stable Localization to the Plasma Membrane
J. Biochem., June 1, 2009; 145(6): 709 - 720.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.