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J. Biol. Chem., Vol. 276, Issue 8, 5739-5744, February 23, 2001
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From the Bacteriorhodopsin, the light-driven proton
pump of Halobacterium salinarum, consists of the membrane
apoprotein bacterioopsin and a covalently bound retinal cofactor. The
mechanism by which retinal is synthesized and bound to bacterioopsin
in vivo is unknown. As a step toward identifying cellular
factors involved in this process, we constructed an in-frame deletion
of brp, a gene implicated in bacteriorhodopsin biogenesis.
In the
brp and blh Are Required for Synthesis of
the Retinal Cofactor of Bacteriorhodopsin in Halobacterium
salinarum*
,
,,
Department of Biomolecular Chemistry,
University of Wisconsin Medical School, Madison, Wisconsin 53706, § Department of Food Microbiology and Toxicology and
¶ Department of Bacteriology, University of Wisconsin, Madison,
Wisconsin 53706, ** Department of Microbiology, University of
Massachusetts, Amherst, Massachusetts 01003, and Institute
for Systems Biology, Seattle, Washington 98105
brp strain, bacteriorhodopsin levels are
decreased ~4.0-fold compared with wild type, whereas bacterioopsin
levels are normal. The probable precursor of retinal, 
-carotene, is
increased ~3.8-fold, whereas retinal is decreased by ~3.7-fold.
These results suggest that brp is involved in retinal synthesis. Additional cellular factors may substitute for
brp function in the brp strain because
retinal production is not abolished. The in-frame deletion of
blh, a brp paralog identified by analysis of
the Halobacterium sp. NRC-1 genome, reduced
bacteriorhodopsin accumulation on solid medium but not in liquid.
However, deletion of both brp and blh abolished
bacteriorhodopsin and retinal production in liquid medium, again
without affecting bacterioopsin accumulation. The level of -carotene
increased ~5.3-fold. The simplest interpretation of these results is
that brp and blh encode similar proteins that catalyze or regulate the conversion of -carotene to retinal.
*
This work was supported by National Science Foundation Grant
MCB-9983120 (to M. P. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 608-265-5491;
Fax: 608-262-5253; E-mail: mpkrebs@facstaff.wisc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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