spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Deckers-Hebestreit, G.
Right arrow Articles by Altendorf, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Deckers-Hebestreit, G.
Right arrow Articles by Altendorf, K.

Journal of Experimental Biology, Vol 172, Issue 1 451-459, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

The Fo complex of the proton-translocating F-type ATPase of Escherichia coli

G Deckers-Hebestreit and K Altendorf
Universitat Osnabruck, Fachbereich Biologie/Chemie, Arbeitsgruppe Mikrobiologie, FRG.

The ATP synthase (F1Fo) of Escherichia coli consists of two structurally and functionally distinct entities. The F1 part is composed of five subunits alpha, beta, gamma, delta and epsilon (3:3:1:1:1) and carries the catalytic centres of the enzyme. The membrane-bound Fo complex functions as a proton channel and consists of the three subunits a, b and c (1:2:10 +/- 1). Subunit c (8288 M(r)) exhibits a hairpin-like structure within the membrane. A conserved acidic residue (Asp-61) in the C-terminal hydrophobic segment is absolutely required for proton translocation through Fo, whereas the hydrophilic loop region is necessary for F1 binding. Expression of the chloroplast proteolipid together with subunits a and b of E. coli did not produce an active Fo hybrid complex. Therefore, the construction of hybrid c subunits consisting of parts of the proteolipid from both organisms is in progress to determine those parts of subunit c that are essential for a functional interplay with subunits a and b. Subunit a (30,276 M(r)), which is also involved in proton translocation, is an extremely hydrophobic protein with 5-8 membrane-spanning helices. Studies with alkaline phosphatase fusion proteins resulted in controversial conclusions about the localization of the N and C termini of the protein. A foreign epitope (13 amino acids) has been inserted into the N- or C-terminal region of subunit a without affecting the function of Fo. Binding studies with a monoclonal antibody against this epitope are now under investigation to determine the orientation of subunit a.(ABSTRACT TRUNCATED AT 250 WORDS)


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Lepier, R. Gräf, M. Azuma, H. Merzendorfer, W. R. Harvey, and H. Wieczorek
The Peripheral Complex of the Tobacco Hornworm V-ATPase Contains a Novel 13-kDa Subunit G
J. Biol. Chem., April 5, 1996; 271(14): 8502 - 8508.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1992