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PMID: 2142688 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Subunit interactions within the chloroplast ATP synthase (CF0-CF1) as deduced by specific depletion of CF0 polypeptides.

The Journal of biological chemistry ·Vol. 265 ·No. 21 ·1990-07-25 ·Pages 12481-5

Feng Y, McCarty RE

Abstract

The proton-linked ATP synthase (CF1-CF0) of chloroplasts consists of a catalytic component (CF1) and a membrane-embedded part (CF0) that interacts with CF1 and contains a proton channel. The subunits of CF0 which are involved in binding of CF1 were studied by examining the effect of selective depletion of subunits I, II, and IV of CF0 from the chloroplast ATP synthase on the association of the remaining CF0 subunits with CF1. Dissociated CF0 subunits were identified by sucrose density gradient centrifugation. Removal of subunit IV alone from CF0-CF1 did not cause dissociation of the other CF0 subunits from CF1. Upon removal of both subunits I and IV from CF0-CF1, subunit II also dissociated, but subunit III was still bound to CF1. Thus, at least two subunits of CF0, I and III, directly associate with CF1. Subunit II is unlikely to bind CF1 directly and may associate with subunit I. Although depletion of subunit IV does not cause dissociation of CF0 from CF1, its interaction with CF1 subunits is uncertain.

MeSH Terms
Chloroplasts/enzymology Dicyclohexylcarbodiimide/metabolism Electrophoresis, Polyacrylamide Gel Macromolecular Substances Plants Protein Binding Proton-Translocating ATPases/physiology Structure-Activity Relationship
Chemicals
Macromolecular Substances Dicyclohexylcarbodiimide Proton-Translocating ATPases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Feng Y
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
McCarty R E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1990-07-25
Pages
12481-5
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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