ArticleJournal of bacteriology1998
Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 121 citations in OpenAlex.
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- Diversification of Phage-Displayed Peptide Libraries with Noncanonical Amino Acid Mutagenesis and Chemical Modification.Chemical reviews · 2024Review
- Phylogenetic and ecophysiological novelty of subsurface mercury methylators in mangrove sediments.The ISME journal · 2023Article
- A diversified, widespread microbial gene cluster encodes homologs of methyltransferases involved in methanogenesis.bioRxiv : the preprint server for biology · 2023Article
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- The methanogen core and pangenome: conservation and variability across biology's growth temperature extremes.DNA research : an international journal for rapid publication of reports on genes and genomes · 2023Article
- Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.Communications biology · 2023Article
- Conserved and lineage-specific hypothetical proteins may have played a central role in the rise and diversification of major archaeal groups.BMC biology · 2022Article
- Metaproteomics reveals methyltransferases implicated in dichloromethane and glycine betaine fermentation by 'Frontiers in microbiology · 2022Article
- Translational accuracy of a tethered ribosome.Nucleic acids research · 2021Article
- An Ecological Basis for Dual Genetic Code Expansion in Marine Deltaproteobacteria.Frontiers in microbiology · 2021Article
- Channeling C1 Metabolism towardmBio · 2020Article
- Retroconversion of estrogens into androgens by bacteria via a cobalamin-mediated methylation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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