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PMID: 2531737 Published · ppublish English Comparative Study Journal Article Review

Structure, molecular genetics, and evolution of vacuolar H+-ATPases.

Journal of bioenergetics and biomembranes ·Vol. 21 ·No. 5 ·1989-10-00 ·Pages 553-71

Nelson N

Abstract

Proton-ATPases can be divided into three classes denoted as P-, F-, and V-ATPases. The P-ATPases are evolutionarily distinct from the F- and V-type ATPases which have been shown to be related, probably evolved from a common ancestral enzyme. Like F-ATPases, V-ATPases are composed of two distinct structures: a catalytic sector that is hydrophilic in nature and a hydrophobic membrane sector which functions in proton conduction. Recent studies on the molecular biology of vacuolar H+-ATPases revealed surprising findings about the evolution of pronon pumps as well as important clues for the evolution of eukaryotic cells.

MeSH Terms
Amino Acid Sequence Animals Bacteria/enzymology,genetics Biological Evolution Cattle Chromaffin Granules/enzymology Escherichia coli/enzymology,genetics Molecular Sequence Data Proton-Translocating ATPases/genetics Saccharomyces cerevisiae/enzymology,genetics Sequence Homology, Nucleic Acid Vacuoles/enzymology
Chemicals
Proton-Translocating ATPases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Nelson N
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00808113
Published
1989-10-00
Pages
553-71
Language
English
Region
United States
NLM ID
7701859
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00808113 View journal details
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