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Journal of Bacteriology, January 1999, p. 662-665, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
S-Methylmethionine Metabolism in
Escherichia coli
Martin
Thanbichler,
Bernhard
Neuhierl, and
August
Böck*
Lehrstuhl für Mikrobiologie der
Universität München, D-80638 Munich, Germany
Received 6 August 1998/Accepted 6 November 1998
Selenium-accumulating Astragalus spp. contain an enzyme
which specifically transfers a methyl group from
S-methylmethionine to the selenol of selenocysteine, thus
converting it to a nontoxic, since nonproteinogenic, amino acid.
Analysis of the amino acid sequence of this enzyme revealed that
Escherichia coli possesses a protein (YagD) which shares
high sequence similarity with the enzyme. The properties and
physiological role of YagD were investigated. YagD is an
S-methylmethionine: homocysteine methyltransferase which
also accepts selenohomocysteine as a substrate. Mutants in
yagD which also possess defects in metE and
metH are unable to utilize S-methylmethionine
for growth, whereas a metE metH double mutant still grows
on S-methylmethionine. Upstream of yagD and
overlapping with its reading frame is a gene (ykfD) which, when inactivated, also blocks growth on methylmethionine in a metE metH genetic background. Since it displays sequence
similarities with amino acid permeases it appears to be the transporter
for S-methylmethionine. Methionine but not
S-methylmethionine in the medium reduces the amount of
yagD protein. This and the existence of four MET box motifs
upstream of yfkD indicate that the two genes are members of
the methionine regulon. The physiological roles of the ykfD
and yagD products appear to reside in the acquisition of
S-methylmethionine, which is an abundant plant product, and its utilization for methionine biosynthesis.
*
Corresponding author. Mailing address: Institute of
Genetics and Microbiology, Maria-Ward-Strasse 1a, D-80638 Munich,
Germany. Phone: 89-17919856. Fax: 89-17919863. E-mail:
august.boeck{at}lrz.uni-muenchen.de.
Journal of Bacteriology, January 1999, p. 662-665, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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