DEMONSTRATION THAT THE BCHH PROTEIN OF RHODOBACTER-CAPSULATUS ACTIVATES S-ADENOSYL-L-METHIONINE-MAGNESIUM PROTOPORPHYRIN-IX METHYLTRANSFERASE

The bchH gene of Rhodobacter capsulatus has been cloned into an expres sion strain of Escherichia coli. Following induction of expression of the BchH protein, it was found that the E. coli strain also accumulate d porphyrins with the fluorescence properties of protoporphyrin and zi nc protoporphyrin. It was also found that the soluble BchH protein inc reased the activity of S-adenosyl-L-methionine:magnesium protoporphyri n IX methyltransferase, when mixed with membranes of an expression str ain of E. coli into which the bchM gene (which encodes the methyltrans ferase) had been cloned, as well as membranes of a bchH mutant of R. c apsulatus. (C) 1997 Federation of European Biochemical Societies.