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The prokaryote-to-eukaryote transition reflected in the evolution of the V/F/A-ATPase catalytic and proteolipid subunitsChanges in the primary and quarternary structure of vacuolar and archaeal type ATPases that accompany the prokaryote-to-eukaryote transition are analyzed. The gene encoding the vacuolar-type proteolipid of the V-ATPase from Giardia lamblia is reported. Giardia has a typical vacuolar ATPase as observed from the common motifs shared between its proteolipid subunit and other eukaryotic vacuolar ATPases, suggesting that the former enzyme works as a hydrolase in this primitive eukaryote. The phylogenetic analyses of the V-ATPase catalytic subunit and the front and back halves of the proteolipid subunit placed Giardia as the deepest branch within the eukaryotes. Our phylogenetic analysis indicated that at least two independent duplication and fusion events gave rise to the larger proteolipid type found in eukaryotes and in Methanococcus. The spatial distribution of the conserved residues among the vacuolar-type proteolipids suggest a zipper-type interaction among the transmembrane helices and surrounding subunits of the V-ATPase complex. Important residues involved in the function of the F-ATP synthase proteolipid have been replaced during evolution in the V-proteolipid, but in some cases retained in the archaeal A-ATPase. Their possible implication in the evolution of V/F/A-ATPases is discussed.
Document ID
20040172656
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Hilario, E.
(University of Connecticut 75 N. Eagleville Road, Storrs, CT 06269-3044, United States)
Gogarten, J. P.
Date Acquired
August 22, 2013
Publication Date
June 1, 1998
Publication Information
Publication: Journal of molecular evolution
Volume: 46
Issue: 6
ISSN: 0022-2844
Subject Category
Exobiology
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Exobiology
Non-NASA Center

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