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. 1982 Jul;151(1):127–134. doi: 10.1128/jb.151.1.127-134.1982

Identification of a protein of 15,000 daltons related to isoleucine-valine biosynthesis in Escherichia coli K-12.

J E Gray, J W Wallen, D H Calhoun
PMCID: PMC220212  PMID: 6211430

Abstract

The effect of the ilvG671, ilvG468, and ilvG603 mutations (phenotype, IlvG+ Valr; formerly ilvO) upon proteins synthesized was determined by infection of irradiated Escherichia coli K-12 cells, using specifically constructed derivatives of lambda dilv phage. These ilvG alleles are similar to the previously studied ilvG2096(Valr) allele in that they activate the latent ilvG gene which is present in the wild-type strain, leading to the synthesis of a 62,000-dalton protein. In addition, all of these ilvG (Valr) alleles increase the synthesis of a 15,000-dalton protein. To localize the gene coding for the 15,000-dalton protein, the proteins produced in maxicells containing plasmids with specific deletions of ilv and rrnX DNA segments were analyzed. The gene coding for the 15,000-dalton protein was located within a region about 1,000 base pairs long between ilv and trpT. The function of the 15,000-dalton protein is not known.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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