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Journal of Bacteriology, May 2009, p. 3407-3410, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01722-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Oxidation of Cysteine 645 of Cobalamin-Independent Methionine Synthase Causes a Methionine Limitation in Escherichia coli{triangledown} ,{dagger}

Elise R. Hondorp1* and Rowena G. Matthews1,2

Life Sciences Institute,1 Department of Biological Chemistry and Biophysics Research Division, The University of Michigan, 210 Washtenaw Ave., Ann Arbor, Michigan 48109-22162

Received 9 December 2008/ Accepted 7 March 2009

Cobalamin-independent methionine synthase (MetE) catalyzes the final step in Escherichia coli methionine biosynthesis but is inactivated under oxidative conditions, triggering a methionine deficiency. This study demonstrates that the mutation of MetE cysteine 645 to alanine completely eliminates the methionine auxotrophy imposed by diamide treatment, suggesting that modulation of MetE activity via cysteine 645 oxidation has significant physiological consequences for oxidatively stressed cells.

* Corresponding author. Present address: 3213 Biosciences Research Bldg., Department of Cell Biology & Molecular Genetics and Maryland Pathogen Research Institute, University of Maryland, College Park, MD 20742. Phone: (301) 405-7514. Fax: (301) 314-1248. E-mail: ehondorp{at}umd.edu

{triangledown} Published ahead of print on 13 March 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, May 2009, p. 3407-3410, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01722-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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