ISSN:
1573-6881
Keywords:
archaea
;
methanogens
;
bioenergetics
;
ATPases
;
ATP synthases
;
evolution
;
proteolipids
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract Recent molecular studies revealed nine to ten gene products involved infunction/assembly of the methanoarchaeal ATPase and unravel a closerelationship of the A1A0-ATPase and theV1V0-ATPase with respect to subunit composition and thestructure of individual subunits. Most interestingly, there is anastonishing variability in the size of the proteolipids in methanoar chaealA1A0-ATPases with six, four, or two transmembranehelices and a variable number of conserved protonizable groups per monomer.Despite the structural similarities the A1A0-ATPasediffers fundamentally from the V1V0-ATPase by itsability to synthesize ATP, a feature shared withF1F0-ATPases. The discovery of duplicated andtriplicated versions of the proteolipid in A1A0-ATPsynthases questions older views of the structural requirements for ATPsynthases versus ATP hydrolases and sheds new light on the evolutionof these secondary energy converters.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005451311009
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