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J Biol Chem, Vol. 274, Issue 36, 25827-25832, September 3, 1999
From Biochemistry and Genetics, The Medical School, University of
Newcastle, NE2 4HH, United Kingdom
CoaR associates with and confers
cobalt-dependent activation of the coaT
operator-promoter. A CoaR mutant (Ser-Asn-Ser) in a carboxyl-terminal
Cys-His-Cys motif bound the coaT operator-promoter but did
not activate expression in response to cobalt, implicating thiolate
and/or imidazole ligands at these residues in an allosteric cobalt
binding site. Deletion of 1 or 2 nucleotides from between near
consensus, but with aberrant (20 base pairs) spacing, 
10 and 35
elements enhanced expression from the coaT
operator-promoter but abolished activation by cobalt-CoaR. It is
inferred that cobalt effects a transition in CoaR that underwinds the
coaT operator-promoter to realign promoter elements. In the
absence of cobalt, CoaR represses expression (~50%). CoaR is a
fusion of ancestral MerR (mercury-responsive transcriptional
activator)- and precorrin isomerase (enzyme of vitamin B12
biosynthesis)-related sequences. Expression from the coaT
operator-promoter was enhanced in a partial mutant of cbiE (encoding an enzyme preceding precorrin isomerase in B12
biosynthesis), revealing that this pathway "inhibits"
coaT expression. Disruption of coaT reduced
cobalt tolerance and increased cytoplasmic 57Co
accumulation. coaT-mediated restoration of cobalt tolerance has been used as a selectable marker.
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