Abstract
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 I1vI (larger subunit of AHAS III) and I1vG (larger subunit of AHAS II) polypeptides. There is less size uniformity among the I1vN, I1vH (smaller subunit of AHAS III), and I1vM (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.
MeSH Terms
Acetolactate Synthase/genetics
Amino Acid Sequence
Base Sequence
DNA Restriction Enzymes
Escherichia coli/enzymology,genetics
Genes
Genes, Bacterial
Macromolecular Substances
Molecular Weight
Operon
Oxo-Acid-Lyases/genetics
Transcription, Genetic
Chemicals
Macromolecular Substances
Acetolactate Synthase
DNA Restriction Enzymes
Oxo-Acid-Lyases
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Friden P
Donegan J
Mullen J
Tsui P
Freundlich M
Eoyang L
Weber R
Silverman P M
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