HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Daas, P. J.H. Articles by Vogels, G. D. Search for Related Content PubMed PubMed Citation Articles by Daas, P. J.H. Articles by Vogels, G. D. Social Bookmarking                      What's this?

Volume 271, Number 37, Issue of September 13, 1996 pp. 22339-22345
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Purification and Properties of an Enzyme Involved in the ATP-dependent Activation of the Methanol:2-Mercaptoethanesulfonic Acid Methyltransferase Reaction in Methanosarcina barkeri

(Received for publication, December 29, 1995, and in revised form, June 7, 1996)

From the Department of Microbiology, Faculty of Science, University of Nijmegen, Toernooiveld, NL-6525 ED Nijmegen, The Netherlands

In Methanosarcina barkeri the transfer of the methyl group from methanol to 2-mercaptoethanesulfonic acid is catalyzed by the concerted action of two methyltransferases. The first one is the corrinoid-containing methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MT₁), which binds the methyl group of methanol to its corrinoid prosthetic group. MT₁ is only catalytically active when the cobalt atom of the corrinoid is present in the highly reduced Co(I) state. In the course of its purification and even during catalysis, MT₁ becomes oxidatively inactivated. The enzyme, however, may be reductively reactivated by a suitable reducing system (hydrogen and hydrogenase), ATP, and an enzyme called methyltransferase activation protein (MAP). In order to elucidate its role in the reactivation process, MAP was purified to apparent homogeneity. The protein had an M_r = 60,000. Preincubation of the enzymic components involved with 8-azido-ATP or with ATP demonstrated MAP to be the primary site of action of ATP. In agreement herewith, the protein was autophosphorylated by [-³²P]ATP in a 1:1 stoichiometry. Phosphorylated MAP substituted for ATP in the activation of MT₁, and the addition of increasing amounts of MAP phosphate resulted in a corresponding increase of active MT₁. However, in the presence of limiting amounts of MAP, maximal activation of MT₁ could be achieved during a lag phase provided ATP was present, indicating that MAP acts as a catalyst. This paper is the first to report on the presence, isolation, and function of a phosphorylated protein in a methanogenic archaeon.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				W. F. Fricke, H. Seedorf, A. Henne, M. Kruer, H. Liesegang, R. Hedderich, G. Gottschalk, and R. K. Thauer The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H2 for Methane Formation and ATP Synthesis J. Bacteriol., January 15, 2006; 188(2): 642 - 658. [Abstract] [Full Text] [PDF]

				J. Eichler and M. W. W. Adams Posttranslational Protein Modification in Archaea Microbiol. Mol. Biol. Rev., September 1, 2005; 69(3): 393 - 425. [Abstract] [Full Text] [PDF]

				W. K. Ray, S. M. Keith, A. M. DeSantis, J. P. Hunt, T. J. Larson, R. F. Helm, and P. J. Kennelly A Phosphohexomutase from the Archaeon Sulfolobus solfataricus Is Covalently Modified by Phosphorylation on Serine J. Bacteriol., June 15, 2005; 187(12): 4270 - 4275. [Abstract] [Full Text] [PDF]

				B. H. Lower, M. B. Potters, and P. J. Kennelly A Phosphoprotein from the Archaeon Sulfolobus solfataricus with Protein-Serine/Threonine Kinase Activity J. Bacteriol., January 15, 2004; 186(2): 463 - 472. [Abstract] [Full Text] [PDF]

				M. Unciuleac and M. Boll Mechanism of ATP-driven electron transfer catalyzed by the benzene ring-reducing enzyme benzoyl- CoA reductase PNAS, October 31, 2001; (2001) 241375598. [Abstract] [Full Text] [PDF]

				T. Vannelli, M. Messmer, A. Studer, S. Vuilleumier, and T. Leisinger A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane PNAS, April 13, 1999; 96(8): 4615 - 4620. [Abstract] [Full Text] [PDF]

				S. A. Burke, S. L. Lo, and J. A. Krzycki Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine J. Bacteriol., July 1, 1998; 180(13): 3432 - 3440. [Abstract] [Full Text]

				S. A. Burke and J. A. Krzycki Reconstitution of Monomethylamine:Coenzyme M Methyl Transfer with a Corrinoid Protein and Two Methyltransferases Purified from Methanosarcina barkeri J. Biol. Chem., June 27, 1997; 272(26): 16570 - 16577. [Abstract] [Full Text] [PDF]

				D. J. Ferguson Jr., N. Gorlatova, D. A. Grahame, and J. A. Krzycki Reconstitution of Dimethylamine:Coenzyme M Methyl Transfer with a Discrete Corrinoid Protein and Two Methyltransferases Purified from Methanosarcina barkeri J. Biol. Chem., September 8, 2000; 275(37): 29053 - 29060. [Abstract] [Full Text] [PDF]

				M. Unciuleac and M. Boll Mechanism of ATP-driven electron transfer catalyzed by the benzene ring-reducing enzyme benzoyl- CoA reductase PNAS, November 20, 2001; 98(24): 13619 - 13624. [Abstract] [Full Text] [PDF]