Abstract

CONTENT ALERTS Receive: RSS Feeds, eTOCs, free email alerts (when new articles cite this article), more» Information about commercial reprint orders: http://jb.asm.org/site/misc/reprints.xhtml To subscribe to to another ASM Journal go to: http://journals.asm.org/site/subscriptions/ JOURNAL OF BACTERIOLOGY, June 1992, p. 3824-3825 Vol. 174, No. 11 0021-9193/92/113824-02$02.00/0 Copyright X 1992, American Society for Microbiology JOHN M. DELANEY* AND COSTA GEORGOPOULOS Department of Cellular, Viral, and Molecular Biology, School of Medicine, University of Utah, Salt Lake City, Utah 84132 The Escherichia coli thioredoxin reductase enzyme is a flavoprotein which catalyzes the transfer of reducing potential from NADPH to thioredoxin (4, 9).Thioredoxin participates in the reduction of ribonucleotides during DNA biosynthesis in E. coli (9) and is essential for sulfate reduction during cysteine biosynthesis (8, 9). In addition, thioredoxin functions in vitro in the reduction ofmethionine sulfoxide and protein disulfides (9). An E. coli mutant deficient in thioredoxin reductase activity has been isolated, defining the trxB gene (4). The trxB gene has been genetically mapped to ment the HtrD Ts- phenotype. Further analysis of subclones precisely localized the htrD gene to a position centered around kb 942.5 on the E. coli physical map (Fig. 1) (7). Sequence analysis of the htrD gene (to