Threonine deaminase: autogenous regulator of the ilv genes in Escherichia coli K-12

Abstract

In this paper we analyze the effect of mutations in three genes, ilvO, ilvA and rho, on the expression of the ilvEJGDA gene cluster of Escherichia coli K-12. The ilvO603 mutation causes a cis-dominant derepression of the ilvEJGDA genes. In particular, the ilvG gene, not expressed in the wild type, becomes expressed in the ilvO603 strain. We have introduced ilvA mutations (ilvA454 or ilvA628) in the ilvO603 strain and we show that ilvG expression requires the presence in cis of both an ilvO603 mutation and of an ilvA+ allele. The ilvG gene is not expressed when in trans is present an ilvO+, ilvA+ genotype. However, it is expressed when the chromosome in trans is ilvO603, ilvA+ (ilvG-). We suggest that ilvO603 is part of ilvA, the structural gene for threonine deaminase, and that threonine deaminase from the ilvO603 mutant binds the ilvO603 site and not the ilvO+ site. Therefore, the ilvA gene product would be a cis-acting protein. Mutations in the rho gene cause derepression of the ilvEJGDA gene cluster without a concomitant expression of the ilvG gene. We show that introduction of either a rho-218 or a rho-115 mutation into the ilvO603, ilvA454 double mutant causes expression of ilvG. We therefore suggest that the ilvA gene product, threonine deaminase, is involved in termination of transcription as an antagonist of the rho gene product. Introduction of ilvA454 into an ilvO603 strain causes also a decrease in expression of the ilvE, ilvJ and ilvD genes. This effect is maximum in the case of the ilvD gene and we studied it in detail in isogenic strains containing also the rho-218 mutation.