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ubo
ová,
Kathleen Sandman,
Elizabeth A. Karr,
Andrew J. Cochran, and
John N. Reeve*
Department of Microbiology, Ohio State University, Columbus, Ohio 43210-1292
Received 31 January 2007/ Accepted 19 March 2007
Over 90% of Methanothermobacter thermautotrophicus mutants isolated as spontaneously resistant to 5-methyl tryptophan had mutations in trpY. Most were single-base-pair substitutions that identified separate DNA- and tryptophan-binding regions in TrpY. In vivo and in vitro studies revealed that DNA binding was sufficient for TrpY repression of trpY transcription but that TrpY must bind DNA and tryptophan to assemble a complex that represses trpEGCFBAD.
Published ahead of print on 30 March 2007.
Permanent address: Institute of Animal Biochemistry and Genetics, Ivanka Pri Dunaji, Slovak Republic.
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