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The evolution of energy-transducing systems. Studies with an extremely halophilic archaebacteriumThe halobacterial ATPase was labeled with C-14-dicyclohexylcarbodiimide and subunit 2 of the enzyme was prepared by electroelution. Subunit 2 was cleaved by several chemical and enzymatic procedures for further preparation of peptides. Immunoreactions (Western blotting) of halobacterial membranes were performed with an antiserum against subunit A of the vacuolar ATPase from Neurospora crassa. A 85 K band (subunit 1) from the membranes of H saccharovorum and from two halobacterial isolates, which were isolated from Permian salt sediments, reacted strongly with the antiserum. The ATPase from the latter isolates resembled the ATPase from H saccharovorum, but had a higher content of acidic amino acids. If it can be verified that the age of the bacterial isolates is in the same range as when deposition of salt occurred, an extremely interesting system for the study of evolutionary questions would be available, since the salt-embedded bacteria presumably did not undergo mutational and selectional events.
Document ID
19910018410
Acquisition Source
Legacy CDMS
Document Type
Contractor Report (CR)
Authors
Stan-Lotter, Helga (NASA Ames Research Center Moffett Field, CA, United States)
Date Acquired
September 6, 2013
Publication Date
July 1, 1991
Subject Category
Life Sciences (General)
Report/Patent Number
NASA-CR-188641
NAS 1.26:188641
Accession Number
91N27724
Funding Number(s)
CONTRACT_GRANT: NCC2-578
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.

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