Vol. 180, Issue 13, 3432-3440, July 1, 1998
Department of Microbiology, Ohio State
University, Columbus, Ohio 43210
Coenzyme M (CoM) is methylated during methanogenesis from
monomethyamine in a reaction catalyzed by three proteins. Using monomethylamine, a 52-kDa polypeptide termed monomethylamine
methyltransferase (MMAMT) methylates the corrinoid cofactor bound to a
second polypeptide, monomethylamine corrinoid protein (MMCP).
Methylated MMCP then serves as a substrate for MT2-A, which methylates
CoM. The genes for these proteins are clustered on 6.8 kb of DNA in
Methanosarcina barkeri MS. The gene encoding MMCP
(mtmC) is located directly upstream of the gene encoding
MMAMT (mtmB). The gene encoding MT2-A (mtbA)
was found 1.1 kb upstream of mtmC, but no obvious open
reading frame was found in the intergenic region between mtbA and mtmC. A single monocistronic
transcript was found for mtbA that initiated 76 bp from the
translational start. Separate transcripts of 2.4 and 4.7 kb were
detected, both of which carried mtmCB. The larger
transcript also encoded mtmP, which is homologous to the
APC family of cationic amine permeases and may therefore encode a
methylamine permease. A single transcriptional start site was found 447 bp upstream of the translational start of mtmC. MtmC
possesses the corrinoid binding motif found in corrinoid proteins
involved in dimethylsulfide- and methanol-dependent methanogenesis, as
well as in methionine synthase. The open reading frame of
mtmB was interrupted by a single in-frame, midframe, UAG
codon which was also found in mtmB from M. barkeri NIH. A mechanism that circumvents UAG-directed
termination of translation must operate during expression of
mtmB in this methanogen.
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