Document Detail


The C-terminal domain of the epsilon subunit of the chloroplast ATP synthase is not required for ATP synthesis.
MedLine Citation:
PMID:  12484749     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The epsilon subunit of the ATP synthases from chloroplasts and Escherichia coli regulates the activity of the enzyme and is required for ATP synthesis. The epsilon subunit is not required for the binding of the catalytic portion of the chloroplast ATP synthase (CF1) to the membrane-embedded part (CFo). Thylakoid membranes reconstituted with CF1 lacking its epsilon subunit (CF1-epsilon) have high ATPase activity and no ATP synthesis activity, at least in part because the membranes are very leaky to protons. Either native or recombinant epsilon subunit inhibits ATPase activity and restores low proton permeability and ATP synthesis. In this paper we show that recombinant epsilon subunit from which 45 amino acids were deleted from the C-terminus is as active as full-length epsilon subunit in restoring ATP synthesis to membranes containing CF1-epsilon. However, the truncated form of the epsilon subunit was significantly less effective as an inhibitor of the ATPase activity of CF1-epsilon, both in solution and bound to thylakoid membranes. Thus, the C-terminus of the epsilon subunit is more involved in regulation of activity, by inhibiting ATP hydrolysis, than in ATP synthesis.
Authors:
Kristine F Nowak; Vazha Tabidze; Richard E McCarty
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  41     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2002 Dec 
Date Detail:
Created Date:  2002-12-17     Completed Date:  2003-02-06     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15130-4     Citation Subset:  IM    
Affiliation:
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218-2685, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / biosynthesis*
Ca(2+) Mg(2+)-ATPase / antagonists & inhibitors
Calcium-Transporting ATPases / antagonists & inhibitors
Chloroplast Proton-Translocating ATPases / antagonists & inhibitors,  chemistry*,  genetics
Enzyme Inhibitors / chemistry
Light
Peptide Fragments / chemistry*,  genetics
Plant Proteins / chemistry*,  genetics
Protein Structure, Tertiary / genetics
Protein Subunits / chemistry*,  genetics
Proteins / chemistry*,  genetics
Recombinant Proteins / chemistry
Spectrometry, Fluorescence
Spinacia oleracea / enzymology,  genetics
Thylakoids / enzymology,  genetics
Chemical
Reg. No./Substance:
0/ATPase inhibitory protein; 0/Enzyme Inhibitors; 0/Peptide Fragments; 0/Plant Proteins; 0/Protein Subunits; 0/Proteins; 0/Recombinant Proteins; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Ca(2+) Mg(2+)-ATPase; EC 3.6.1.8/Calcium-Transporting ATPases; EC 3.6.3.-/Chloroplast Proton-Translocating ATPases

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