JBC INTERFERin siRNA transfection reagent

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Volume 270, Number 4, Issue of January 27, 1995 pp. 1489-1492
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Construction and Function of Chimeric Subunits Containing Regions from the Subunits of the FF ATPases of Escherichia coli and Bacillus megaterium

(Received for publication, November 1, 1994)

Sharlene R. Matten ,  Randy A. Schemidt,  William S. A. Brusilow

The highly conserved beta subunit of the Escherichia coli F(1)F(0) ATPase was divided into three sections, each of which was exchanged with the homologous section of the beta subunit of the obligate aerobe Bacillus megaterium. Plasmids coding for the resultant six chimeric beta subunits varied in their abilities to complement two E. coli beta mutants as measured by testing transformed cells for aerobic growth on a nonfermentable carbon source or anaerobic growth on rich medium containing glucose. Two chimeras were able to restore both growth on succinate and anaerobic growth on rich medium. The genetic results corresponded to increased levels of membrane-bound ATPase and ATP synthase activities. These chimeric subunits were therefore capable of being assembled into functional E. coli ATPase complexes. The results indicate that chimeric beta subunits can be used to analyze assembly of the beta subunit and that the final 181 amino acids of the beta subunit might contain a region involved in functional energy coupling.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.