Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons.
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.
Carlomagno
M S
MS
Centro di Endocrinologia ed Oncologia, Sperimentale del Consiglio, Nazionale delle Ricerche, University of Naples, Napoli, Italy.
Chiariotti
L
L
Alifano
P
P
Nappo
A G
AG
Bruni
C B
CB
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001483:Base Sequence; D003062:Codon; D004926:Escherichia coli; D005796:Genes; D005798:Genes, Bacterial; D006639:Histidine / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009876:Operon; D012486:Salmonella typhimurium; D014158:Transcription, Genetic
D000596:Amino Acids; D003062:Codon; D006639:Histidine