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J. Bacteriol., Sep 1996, 5279-5290, Vol 178, No. 17
SE Lang, FE Jenney Jr and F Daldal
While searching for components of the soluble electron carrier (cytochrome
c2)-independent photosynthetic (Ps) growth pathway in Rhodobacter
capsulatus, a Ps- mutant (FJM13) was isolated from a Ps+ cytochrome
c2-strain. This mutant could be complemented to Ps+ growth by cycA encoding
the soluble cytochrome c2 but was unable to produce several c-type
cytochromes. Only cytochrome c1 of the cytochrome bc1 complex was present
in FJM13 cells grown on enriched medium, while cells grown on minimal
medium contained at various levels all c-type cytochromes, including the
membrane-bound electron carrier cytochrome cy. Complementation of FJM13 by
a chromosomal library lacking cycA yielded a DNA fragment which also
complemented a previously described Ps- mutant, MT113, known to lack all
c-type cytochromes. Deletion and DNA sequence analyses revealed an open
reading frame homologous to cycH, involved in cytochrome c biogenesis. The
cycH gene product (CycH) is predicted to be a bipartite protein with
membrane-associated amino- terminal (CycH1) and periplasmic
carboxyl-terminal (CycH2) subdomains. Mutations eliminating CyCH
drastically decrease the production or all known c-type cytochromes.
However, mutations truncating only its CycH2 subdomain always produce
cytochrome c1 and affect the presence of other cytochromes to different
degrees in a growth medium-dependent manner. Thus, the subdomain CycH1 is
sufficient for the proper maturation of cytochrome c1 which is the only
known c-type cytochrome anchored to the cytoplasmic membrane by its
carboxyl terminus, while CycH2 is required for efficient biogenesis of
other c-type cytochromes. These findings demonstrate that the two
subdomains of CycH play different roles in the biogenesis of topologically
distinct c-type cytochromes and reconcile the apparently conflicting data
previously obtained for other species.
Copyright © 1996, American Society for Microbiology
Rhodobacter capsulatus CycH: a bipartite gene product with pleiotropic effects on the biogenesis of structurally different c-type cytochromes
Department of Biology, Plant Science Institute, University of Pennsylvania, Philadelphia 19104-6018, USA.
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