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PMID: 8056784 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

The mitochondrial ATP synthase of Trypanosoma brucei: structure and regulation.

Journal of bioenergetics and biomembranes ·Vol. 26 ·No. 2 ·1994-04-00 ·Pages 173-8

Williams N

Abstract

The structure and regulation of the Trypanosoma brucei mitochondrial ATP synthase is reviewed. This enzyme complex which catalyzes the synthesis and hydrolysis of ATP within the mitochondrion is a multisubunit complex which is regulated in several ways. Several lines of evidence have shown that the ATP synthase is regulated through the life cycle of Trypanosoma brucei. The enzyme complex is present at maximal levels in the procyclic form where mitochondrial activity is the highest and cytochromes and Kreb's cycle components are present. The levels of the ATP synthase are decreased in the bloodstream forms where the levels of the mitochondrial cytochromes are absent or substantially decreased. In recent preliminary work we have shown the presence of an ATP synthase inhibitor peptide which may indicate an additional level of complexity to the regulation.

MeSH Terms
Animals Intracellular Membranes/enzymology Mitochondria/enzymology Molecular Structure Proton-Translocating ATPases/chemistry,metabolism Trypanosoma brucei brucei/enzymology,growth & development
Chemicals
Proton-Translocating ATPases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Williams N
Department of Microbiology, State University of New York at Buffalo.
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41 references, click to expand
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00763066
Published
1994-04-00
Pages
173-8
Language
English
Region
United States
NLM ID
7701859
Subset
IM
Grants
NIAID NIH HHS · AI 33694 · United States
External Links
PubMed source DOI: 10.1007/BF00763066 View journal details
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