HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Denda, K. Articles by Yoshida, M. Search for Related Content PubMed PubMed Citation Articles by Denda, K. Articles by Yoshida, M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 33, 17251-17254, Nov, 1988

Molecular cloning of the beta-subunit of a possible non-F0F1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius

K Denda, J Konishi, T Oshima, T Date and M Yoshida
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.

The gene which encodes the beta subunit of the novel membrane- associated ATPase has been identified and characterized. The beta subunit, which is most likely the soluble part of the non-F0F1 type H+- ATPase, was obtained from the archaebacterium, Sulfolobus acidocaldarius. In terms of its location, it follows just after the gene for its alpha subunit. It is comprised of 1398 nucleotides, corresponding to a protein of 465 amino acids, and the consensus sequence in the nucleotide binding proteins is poorly conserved. Together with previously described results, the distant homology of the S. acidocaldarius ATPase alpha and beta subunits when compared to those of F0F1-ATPases indicates that this archaebacterial ATPase belongs to an ion-translocating ATPase family uniquely different than F0F1-ATPases even if S. acidocaldarius ATPase and F0F1-ATPases have been derived from a common ancestral ATPase.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. Steinert, V. Wagner, P. G. Kroth-Pancic, and S. Bickel-Sandkotter Characterization and Subunit Structure of the ATP Synthase of the Halophilic Archaeon Haloferax volcanii and Organization of the ATP Synthase Genes J. Biol. Chem., March 7, 1997; 272(10): 6261 - 6269. [Abstract] [Full Text] [PDF]

				R. Wilms, C. Freiberg, E. Wegerle, I. Meier, F. Mayer, and V. Muller Subunit Structure and Organization of the Genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1 J. Biol. Chem., August 2, 1996; 271(31): 18843 - 18852. [Abstract] [Full Text] [PDF]

				S.-B. Peng, B. P. Crider, S. J. Tsai, X.-S. Xie, and D. K. Stone Identification of a 14-kDa Subunit Associated with the Catalytic Sector of Clathrin-coated Vesicle H[IMAGE]-ATPase J. Biol. Chem., February 9, 1996; 271(6): 3324 - 3327. [Abstract] [Full Text] [PDF]

				Q. Liu, P. M. Kane, P. R. Newman, and M. Forgac Site-directed Mutagenesis of the Yeast V-ATPase B Subunit (Vma2p) J. Biol. Chem., January 26, 1996; 271(4): 2018 - 2022. [Abstract] [Full Text] [PDF]