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Nucleic Acids Research, 1985, Vol. 13, No. 11 3979-3992
© 1985

Articles

The ilvB locus of Escherichia coli K-12 is an operon encoding both subunits of acetohydroxyacid synthase I

P. Friden, J. Donegan, J. Mullen, P. Tsui, M. Freundlich, L. Eoyang, R. Weber and P.M. Silverman*

Department of Biochemistry SUNY, Stony Brook, NY 11794 Department of Molecular Biology, Division of Biological Sciences, Albert Einstein College of Medicine Bronx, NY 10461, USA

*To whom correspondence should be addressed

Received March 4, 1985. Revised April 18, 1985. Accepted April 18, 1985.

The ilvB locus of Escherichia coli K-12 encloses two open reading frames defining polypeptides of 60,000 and 11,200 molecular weight. The entire locus, about 2.3 kb, is co-transcribed as an operon. The molecular weights and amino acid compositions of the presumptive operon polypeptides agree with those of the large and small subunit polypeptides of acetohydroxyacid synthase (AHAS) I, for which ilvB is the structural locus. We reserve the designation ilvB for the promoter proximal (longer) cistron and designate the promoter distal cistron ilvN. The molecular weight and amino acid sequence of the ilvB polypeptide are strikingly similar to those of the Ilvl (larger subunit of AHAS III) and IlvG (larger subunit of AHAS II) polypep-tides. There is less size uniformity among the IlvN, IlvH (smaller sub-unit of AHAS III), and IlvM (smaller subunit of AHAS II) polypeptides. Nevertheless, there is significant amino acid sequence homology among the three small subunit polypeptides. Thus, all three AHAS isozymes of E. coli K-12 probably have a common evolutionary origin


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