Internal promoters of the his operon in Salmonella typhimurium

Schmid, Molly B.; Roth, John R.

doi:10.1128/jb.153.2.1114-1119.1983

Cited by 25 publications

(8 citation statements)

References 22 publications

(24 reference statements)

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“…Contrary to the primary hisGp promoter, the hisBp promoter was also not subject to histidine-specific regulation. The relative efficiencies of the hisBp promoter versus the hisGp promoter in the pKO4 system under different growth conditions are in rather good agreement with published in vivo levels of the histidine biosynthetic enzymes, both in minimal medium (11,29) and under derepressed conditions (36).…”

Section: Discussionsupporting

confidence: 79%

Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon

Grisolia¹,

Riccio²,

Bruni³

1983

J Bacteriol

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The entire histidine operon of Escherichia coli K-12 was cloned in the vector plasmid pBR313, and a complete restriction map of the operon was determined. By using subclones, complementation tests, and enzyme assays, we were able to make a correlation between the physical map and the genetic map of the operon. We determined the sequence of a fragment of DNA 665 base pairs long, comprising the distal portion of the hisC gene, the proximal portion of the hisB gene, and the internal transcription initiation site hisBp. The efficiency of this promoter was assessed under different physiological conditions by cloning the DNA fragment in a recombinant vector system used to study transcriptional regulatory signals. The precise point at which transcription initiates was determined by S1 nuclease mapping.

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Section: Discussionsupporting

confidence: 79%

Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon

Grisolia¹,

Riccio²,

Bruni³

1983

J Bacteriol

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“…histidine biosynthesis. In S. typhimurium and E. coli two internal promoters, hisp2 and hisp3, were identified within the histidine operon (Grisolia et al, 1983;Schmid and Roth, 1983;Carlomagno et al, 1988). Promoter hisp2 enables the additional transcription of the genes his(NB), hisH, hisA, hisF and his(IE), whereas hisp3 enables transcription only of the his(IE) gene.…”

Section: Promotersmentioning

confidence: 99%

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum

Kulis-Horn

Persicke

Kalinowski

2013

Microbial Biotechnology

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l-Histidine biosynthesis is an ancient metabolic pathway present in bacteria, archaea, lower eukaryotes, and plants. For decades l-histidine biosynthesis has been studied mainly in Escherichia coli and Salmonella typhimurium, revealing fundamental regulatory processes in bacteria. Furthermore, in the last 15 years this pathway has been also investigated intensively in the industrial amino acid-producing bacterium Corynebacterium glutamicum, revealing similarities to E. coli and S. typhimurium, as well as differences. This review summarizes the current knowledge of l-histidine biosynthesis in C. glutamicum. The genes involved and corresponding enzymes are described, in particular focusing on the imidazoleglycerol-phosphate synthase (HisFH) and the histidinol-phosphate phosphatase (HisN). The transcriptional organization of his genes in C. glutamicum is also reported, including the four histidine operons and their promoters. Knowledge of transcriptional regulation during stringent response and by histidine itself is summarized and a translational regulation mechanism is discussed, as well as clues about a histidine transport system. Finally, we discuss the potential of using this knowledge to create or improve C. glutamicum strains for the industrial l-histidine production.

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“…This mechanism seems to operate also in the his operon. In fact, the genes beyond hisC are expressed from the internal promoter hisBp (3,20,25,53), and the histidine content of the three proximal genes is rather low in both S. typhimurium and E. coli (hisG, four residues; hisD, five residues; and hisC, three and one residue, respectively) (31, 47; C. B. Bruni, unpublished data).…”

Section: Discussionmentioning

confidence: 99%

Cloning, structure, and expression of the Escherichia coli K-12 hisC gene

Grisolia¹,

Carlomagno²,

Nappo³

et al. 1985

J Bacteriol

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We used an expression vector plasmid containing the Escherichia coli K-12 histidine operon regulatory region to subclone the E. coli hisC gene. Analysis of plasmid-coded proteins showed that hisC was expressed in minicells. A protein with an apparent molecular weight of 38,500 was identified as the primary product of the hisC gene. Expression was under control of the hisGp promoter and resulted in very efficient synthesis (over 100-fold above the wild-type levels) of imidazolylacetolphosphate:L-glutamate aminotransferase, the hisC gene product. The complete nucleotide sequence of the hisC gene has been determined. The gene is 1,071 nucleotides long and codes for a protein of 356 amino acids with only one histidine residue.

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Internal promoters of the his operon in Salmonella typhimurium

Cited by 25 publications

References 22 publications

Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon

Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum

Cloning, structure, and expression of the Escherichia coli K-12 hisC gene

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