Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)

Limauro, Danila; Avitabile, A.; Cappellano, Carmela; Puglia, Anna Maria; Bruni, Carmelo B.

doi:10.1016/0378-1119(91)90241-3

Cited by 14 publications

(22 citation statements)

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“…Human cytosolic alanine aminotransferase is nearly identical to rat Alt(c) (26). HisH, HisC, and His5 are synonymous designations for imidazole acetol phosphate AT from Z. mobilis (Zmo) (19), B. subtilis (Bsu) (22), Halobacterium volcanii (Hvo) (7), E. coli (Eco) (18), S. cerevisiae (Sce) (44), Streptomyces coelicolor (Sco) (35), Acetobacter xylinum (Axy) (63), Lactococcus lactis (Lla) (10), and H. influenzae (Hin) (12). In this group, a partial mycobacterial sequence is also available (23).…”

Section: Functional Divergencementioning

confidence: 99%

Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

1996

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Section: Functional Divergencementioning

confidence: 99%

Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

1996

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“…Although a number of aminotransferases are not essential for growth because of the enzymatic backup attributed to the overlapping specificities of the intracellular repertoire of aminotransferases (18), IAP aminotransferase is essential in all organisms studied. Thus, mutants which lack IAP aminotransferase activity have been shown to be auxotrophic for histidine in Escherichia coli (13), Bacillus subtilis (38), Corynebacterium glutamicum (1a), Halobacterium volcanii (6), and Streptomyces coelicolor (21).…”

mentioning

confidence: 99%

Imidazole acetol phosphate aminotransferase in Zymomonas mobilis: molecular genetic, biochemical, and evolutionary analyses

Zhao

Eddy

et al. 1995

J Bacteriol

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hisH encodes imidazole acetol phosphate (IAP) aminotransferase in Zymomonas mobilis and is located immediately upstream of tyrC, a gene which codes for cyclohexadienyl dehydrogenase. A plasmid containing hisH was able to complement an Escherichia coli histidine auxotroph which lacked the homologous aminotransferase. DNA sequencing of hisH revealed an open reading frame of 1,110 bp, encoding a protein of 40,631 Da. The cloned hisH product was purified from E. coli and estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to have a molecular mass of 40,000 Da. Since the native enzyme had a molecular mass of 85,000 Da as determined by gel filtration, the active enzyme species must be a homodimer. The purified enzyme was able to transaminate aromatic amino acids and histidine in addition to histidinol phosphate. The existence of a single protein having broad substrate specificity was consistent with the constant ratio of activities obtained with different substrates following a variety of physical treatments (such as freeze-thaw, temperature inactivation, and manipulation of pyridoxal 5-phosphate content). The purified enzyme did not require addition of pyridoxal 5-phosphate, but dependence upon this cofactor was demonstrated following resolution of the enzyme and cofactor by hydroxylamine treatment. Kinetic data showed the classic ping-pong mechanism expected for aminotransferases. K m values of 0.17, 3.39, and 43.48 mM for histidinol phosphate, tyrosine, and phenylalanine were obtained. The gene structure around hisH-tyrC suggested an operon organization. The hisH-tyrC cluster in Z. mobilis is reminiscent of the hisH-tyrA component of a complex operon in Bacillus subtilis, which includes the tryptophan operon and aroE. Multiple alignment of all aminotransferase sequences available in the database showed that within the class I superfamily of aminotransferases, IAP aminotransferases (family I␤) are closer to the I␥ family (e.g., rat tyrosine aminotransferase) than to the I␣ family (e.g., rat aspartate aminotransferase or E. coli AspC). Signature motifs which distinguish the IAP aminotransferase family were identified in the region of the active-site lysine and in the region of the interdomain interface.Histidine biosynthesis requires imidazole acetol phosphate aminotransferases (IAP aminotransferases) to catalyze the formation of histidinol phosphate by transamination between imidazole acetol phosphate and glutamate (40). Although a number of aminotransferases are not essential for growth because of the enzymatic backup attributed to the overlapping specificities of the intracellular repertoire of aminotransferases (18), IAP aminotransferase is essential in all organisms studied. Thus, mutants which lack IAP aminotransferase activity have been shown to be auxotrophic for histidine in Escherichia coli (13), Bacillus subtilis (38), Corynebacterium glutamicum (1a), Halobacterium volcanii (6), and Streptomyces coelicolor (21).Genes responsible for histidine biosynthesis form a single operon in Salmonel...

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“…The product of ORF3 is homologous (23% identity) to the histidyl-tRNA synthetase (hisS) of E. coli but lacks about 150 carboxy-terminal amino acids (21). The product of ORF8 is homologous (28% identity) to the Apha-3' enzymes from various microorganisms and contains typical motifs present in these enzymes (26,32,43 (42,30,20). For instance, HIS2 and HIS3 genes, which encode the phosphatase and dehydratase, respectively, map on chromosome R6 and chromosome R15 of S. cerevisiae (7).…”

Section: Cloningmentioning

confidence: 99%

“…Genes encoding the dehydratase in S. coelicolor andA. brasilense have been sequenced and found not to code for the phosphatase (30,20).…”

Section: Cloningmentioning

confidence: 99%

“…The organization of his genes has not been fully determined in any other organism. In Staphylococcus aureus, six of the genes (hisE, -A, -B, -C, -D, and -G) are clustered, whereas in Streptomyces coelicolor, five (and possibly six) genes (hisD, -C, -B, -H, -A, and possibly -F) form an operon and two (hisIE and hisB) are independent (30,36). In Bacillus subtilis, the genes map in two locations, one grouping seven genes (hisA, -B, -D, -F, -G, -C, and -IE) and the other containing a single gene (hisH, corresponding to hisC in E. coli) (11,18,25,37).…”

mentioning

confidence: 99%

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Histidine biosynthesis genes in Lactococcus lactis subsp. lactis

1992

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The genes of Lactococcus lactis subsp. lactis involved in histidine biosynthesis were cloned and characterized by complementation of Escherichia coli and Bacilus subtUlis mutants and DNA sequencing. Complementation of E. coli hisA, hisB, hisC, hisD, hisF, hisG, and hisIE genes and the B. subtilis hisH gene (the E. coli hisC equivalent) allowed localization of the corresponding lactococcal genes. Nucleotide sequence analysis of the 11.5-kb lactococcal region revealed 14 open reading frames (ORFs), 12 of which might form an operon. The putative operon includes eight ORFs which encode proteins homologous to enzymes involved in histidine biosynthesis. The operon also contains (i) an ORF encoding a protein homologous to the histidyl-tRNA synthetases but lacking a motif implicated in synthetase activity, which suggests that it has a role different from tRNA aminoacylation, and (ii) an ORF encoding a protein that is homologous to the 3'-aminoglycoside phosphotransferases but does not confer antibiotic resistance. The remaining ORFs specify products which have no homology with proteins in the EMBL and GenBank data bases.

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Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)

Cited by 14 publications

References 0 publications

Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

Imidazole acetol phosphate aminotransferase in Zymomonas mobilis: molecular genetic, biochemical, and evolutionary analyses

Histidine biosynthesis genes in Lactococcus lactis subsp. lactis

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