This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Burke, S. A.
Right arrow Articles by Krzycki, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burke, S. A.
Right arrow Articles by Krzycki, J. A.

 Previous Article  |  Next Article 

Vol. 180, Issue 13, 3432-3440, July 1, 1998

Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine

Stephen A. Burke, Sam L. Lo, and Joseph A. Krzycki

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.

Copyright © 1998 by American Society for Microbiology


This article has been cited by other articles:

  • Kratzer, C., Carini, P., Hovey, R., Deppenmeier, U. (2009). Transcriptional Profiling of Methyltransferase Genes during Growth of Methanosarcina mazei on Trimethylamine. J. Bacteriol. 191: 5108-5115 [Abstract] [Full Text]  
  • Fournier, G. P., Huang, J., Gogarten, J. P. (2009). Horizontal gene transfer from extinct and extant lineages: biological innovation and the coral of life. Phil Trans R Soc B 364: 2229-2239 [Abstract] [Full Text]  
  • Ferguson, T., Soares, J. A., Lienard, T., Gottschalk, G., Krzycki, J. A. (2009). RamA, a Protein Required for Reductive Activation of Corrinoid-dependent Methylamine Methyltransferase Reactions in Methanogenic Archaea. J. Biol. Chem. 284: 2285-2295 [Abstract] [Full Text]  
  • Schilhabel, A., Studenik, S., Vodisch, M., Kreher, S., Schlott, B., Pierik, A. Y., Diekert, G. (2009). The Ether-Cleaving Methyltransferase System of the Strict Anaerobe Acetobacterium dehalogenans: Analysis and Expression of the Encoding Genes. J. Bacteriol. 191: 588-599 [Abstract] [Full Text]  
  • Bose, A., Pritchett, M. A., Metcalf, W. W. (2008). Genetic Analysis of the Methanol- and Methylamine-Specific Methyltransferase 2 Genes of Methanosarcina acetivorans C2A. J. Bacteriol. 190: 4017-4026 [Abstract] [Full Text]  
  • Herring, S., Ambrogelly, A., Polycarpo, C. R., Soll, D. (2007). Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase. Nucleic Acids Res 35: 1270-1278 [Abstract] [Full Text]  
  • Longstaff, D. G., Larue, R. C., Faust, J. E., Mahapatra, A., Zhang, L., Green-Church, K. B., Krzycki, J. A. (2007). A natural genetic code expansion cassette enables transmissible biosynthesis and genetic encoding of pyrrolysine. Proc. Natl. Acad. Sci. USA 104: 1021-1026 [Abstract] [Full Text]  
  • Soares, J. A., Zhang, L., Pitsch, R. L., Kleinholz, N. M., Jones, R. B., Wolff, J. J., Amster, J., Green-Church, K. B., Krzycki, J. A. (2005). The Residue Mass of L-Pyrrolysine in Three Distinct Methylamine Methyltransferases. J. Biol. Chem. 280: 36962-36969 [Abstract] [Full Text]  
  • Polycarpo, C., Ambrogelly, A., Berube, A., Winbush, S. M., McCloskey, J. A., Crain, P. F., Wood, J. L., Soll, D. (2004). An aminoacyl-tRNA synthetase that specifically activates pyrrolysine. Proc. Natl. Acad. Sci. USA 101: 12450-12454 [Abstract] [Full Text]  
  • Theobald-Dietrich, A., Frugier, M., Giege, R., Rudinger-Thirion, J. (2004). Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA. Nucleic Acids Res 32: 1091-1096 [Abstract] [Full Text]  
  • Srinivasan, G., James, C. M., Krzycki, J. A. (2002). Pyrrolysine Encoded by UAG in Archaea: Charging of a UAG-Decoding Specialized tRNA. Science 296: 1459-1462 [Abstract] [Full Text]  
  • Hao, B., Gong, W., Ferguson, T. K., James, C. M., Krzycki, J. A., Chan, M. K. (2002). A New UAG-Encoded Residue in the Structure of a Methanogen Methyltransferase. Science 296: 1462-1466 [Abstract] [Full Text]  
  • McAnulla, C., Woodall, C. A., McDonald, I. R., Studer, A., Vuilleumier, S., Leisinger, T., Murrell, J. C. (2001). Chloromethane Utilization Gene Cluster from Hyphomicrobium chloromethanicum Strain CM2T and Development of Functional Gene Probes To Detect Halomethane-Degrading Bacteria. Appl. Environ. Microbiol. 67: 307-316 [Abstract] [Full Text]  
  • Paul, L., Ferguson, D. J. Jr., Krzycki, J. A. (2000). The Trimethylamine Methyltransferase Gene and Multiple Dimethylamine Methyltransferase Genes of Methanosarcina barkeri Contain In-Frame and Read-Through Amber Codons. J. Bacteriol. 182: 2520-2529 [Abstract] [Full Text]  
  • Reeve, J. N. (1999). Archaebacteria Then ... Archaes Now (Are There Really No Archaeal Pathogens?). J. Bacteriol. 181: 3613-3617 [Full Text]  
  • Vannelli, T., Messmer, M., Studer, A., Vuilleumier, S., Leisinger, T. (1999). A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane. Proc. Natl. Acad. Sci. USA 96: 4615-4620 [Abstract] [Full Text]  
  • Tallant, T. C., Paul, L., Krzycki, J. A. (2001). The MtsA Subunit of the Methylthiol:Coenzyme M Methyltransferase of Methanosarcina barkeri Catalyses Both Half-reactions of Corrinoid-dependent Dimethylsulfide: Coenzyme M Methyl Transfer. J. Biol. Chem. 276: 4485-4493 [Abstract] [Full Text]  
  • James, C. M., Ferguson, T. K., Leykam, J. F., Krzycki, J. A. (2001). The Amber Codon in the Gene Encoding the Monomethylamine Methyltransferase Isolated from Methanosarcina barkeri Is Translated as a Sense Codon. J. Biol. Chem. 276: 34252-34258 [Abstract] [Full Text]  
  • Ferguson, D. J. Jr., Gorlatova, N., Grahame, D. A., Krzycki, J. A. (2000). Reconstitution of Dimethylamine:Coenzyme M Methyl Transfer with a Discrete Corrinoid Protein and Two Methyltransferases Purified from Methanosarcina barkeri. J. Biol. Chem. 275: 29053-29060 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»