Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons.

Article Details

Citation

Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB

Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons.

J Mol Biol. 1988 Oct 5;203(3):585-606.

PubMed ID
3062174 [ View in PubMed
]
Abstract

We have determined the complete nucleotide sequence of the histidine operons of Escherichia coli and of Salmonella typhimurium. This structural information enabled us to investigate the expression and organization of the histidine operon. The proteins coded by each of the putative histidine cistrons were identified by subcloning appropriate DNA fragments and by analyzing the polypeptides synthesized in minicells. A structural comparison of the gene products was performed. The histidine messenger RNA molecules produced in vivo and the internal transcription initiation sites were identified by Northern blot analysis and S1 nuclease mapping. A comparative analysis of the different transcriptional and translational control elements within the two operons reveals a remarkable preservation for most of them except for the intercistronic region between the first (hisG) and second (hisD) structural genes and for the rho-independent terminator of transcription at the end of the operon. Overall, the operon structure is very compact and its expression appears to be regulated at several levels.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
ATP phosphoribosyltransferaseP60757Details
Histidinol-phosphate aminotransferaseP06986Details
Histidinol dehydrogenaseP06988Details