Histidine biosynthetic pathway and genes: structure, regulation, and evolution.

Alifano, P; Fani, Renato; Liò, P; Lazcano, Antonio; Bazzicalupo, M; Carlomagno, M S; Bruni, C B

doi:10.1128/mmbr.60.1.44-69.1996

Cited by 183 publications

(145 citation statements)

References 195 publications

(350 reference statements)

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“…The fourth step of histidine biosynthesis is performed by 5′ProFAR isomerase. This enzyme catalyses an internal redox reaction converting 5′ProFAR to 5-[(5phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide (PRFAR) (Alifano et al, 1996). The native enzymes from E. coli and S. typhimurium act as monomers (Winkler, 1996).…”

Section: јProfar Isomerase (Hisa)mentioning

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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Section: јProfar Isomerase (Hisa)mentioning

confidence: 99%

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum

Kulis-Horn

Persicke

Kalinowski

2013

Microbial Biotechnology

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“…In the present study, 26S rDNA D1/D2 sequencing was used to characterise a number of food-associated Zygosaccharomyces strains held at the National Collection of Yeast Cultures, the majority of which originally had been identified as Z. rouxii strains by chemotaxonomic methods. Furthermore, sequence analyses were also carried out on the nuclear-encoded ADE2 (encoding phosporibosylaminoimidazole carboxylase), HIS3 (encoding imidazoleglycerol-phosphate dehydratase [17]), and SOD2 (encoding an Na + /H + -antiporter [18]) genes, as well as the mitochondrial-encoded COX2 (also known as COII and encoding subunit II of the cytochrome-c oxidase complex) gene, thus providing a detailed molecular characterisation of this important set of Zygosaccharomyces strains.…”

Section: Introductionmentioning

confidence: 99%

Molecular evidence for the existence of natural hybrids in the genus

James¹,

Bond²,

Stratford³

et al. 2005

FEMS Yeast Research

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26S rDNA D1/D2 sequencing was used to characterise a number of food-associated Zygosaccharomyces rouxii strains held at the National Collection of Yeast Cultures. In the course of this study, four strains (NCYC 1682, NCYC 3042, NCYC 3060 and NCYC 3061) were identified which appeared, based on their D1/D2 sequences, to belong to a novel Zygosaccharomyces species. However, subsequent sequence analysis showed that NCYC 1682, NCYC 3060 and NCYC 3061 possess two highly divergent copies of the nuclear-encoded ADE2, HIS3 and SOD2 genes, indicating these three strains are in fact hybrids. NCYC 3042, however, does appear to represent a novel species which may be hypothesized to have crossed with Z. rouxii and given rise to hybrid strains. Additional approaches to define precise taxonomic status and mechanisms of hybrid genome formation amongst yeast species are discussed.

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“…Two forms of ATP-PRT have been identified that differ in their molecular architecture ( Fig. 1) [2,3]. The long form (HisG L ) has been extensively characterised and is present in most bacteria, fungi and plants [2,[4][5][6][7][8].…”

mentioning

confidence: 99%

Independent catalysis of the short form HisG from Lactococcus lactis

et al. 2016

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Edited by Michael IbbaATP-phosphoribosyltransferase (ATP-PRT) catalyses the first step of histidine biosynthesis. Two different forms of ATP-PRT have been described; the homo-hexameric long form, and the hetero-octameric short form. Lactococcus lactis possesses the short form ATP-PRT comprising four subunits of HisG S , the catalytic subunit, and four subunits of HisZ, a histidyl-tRNA synthetase paralogue. Previous studies have suggested that HisG S requires HisZ for catalysis. Here, we reveal that the dimeric HisG S does display ATP-PRT activity in the absence of HisZ. This result reflects the evolutionary relationship between the long and short form ATP-PRT, which acquired allosteric inhibition and enhanced catalysis via two divergent strategies.

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Histidine biosynthetic pathway and genes: structure, regulation, and evolution.

Cited by 183 publications

References 195 publications

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum

Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum

Molecular evidence for the existence of natural hybrids in the genus

Independent catalysis of the short form HisG from Lactococcus lactis

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