A cluster of four Azospirillum brasilense histidine biosynthetic genes, hisA, hisB, hisF and hisH, was identified on a 4.5 kb DNA fragment and its organization studied by complementation analysis of Escherichia coli mutations and nucleotide sequence. The nucleotide sequence of a 1.3 kb fragment that complemented the E. coli hisB mutation was determined and an ORF of 624 nucleotides which can code for a protein of 207 amino acids was identified. A significant base sequence homology with the carboxy-terminal moiety of the E. coli hisB gene (0.53) and the Saccharomyces cerevisiae HIS3 gene (0.44), coding for an imidazole glycerolphosphate dehydratase activity was found. The amino acid sequence and composition, the hydropathic profile and the predicted secondary structures of the yeast, E. coli and A. brasilense proteins were compared. The significance of the data presented is discussed

Cloning of histidine genes of Azospirillum brasilense: organization of the ABFH genes cluster and nucleotide sequence of the hisB gene / R. Fani; M. Bazzicalupo; G. Damiani; A. Bianchi; C. Schipani; V. Sgaramella; M. Polsinelli. - In: MOLECULAR AND GENERAL GENETICS. - ISSN 0026-8925. - STAMPA. - 216:(1989), pp. 224-229.

Cloning of histidine genes of Azospirillum brasilense: organization of the ABFH genes cluster and nucleotide sequence of the hisB gene

FANI, RENATO;BAZZICALUPO, MARCO;POLSINELLI, MARIO
1989

Abstract

A cluster of four Azospirillum brasilense histidine biosynthetic genes, hisA, hisB, hisF and hisH, was identified on a 4.5 kb DNA fragment and its organization studied by complementation analysis of Escherichia coli mutations and nucleotide sequence. The nucleotide sequence of a 1.3 kb fragment that complemented the E. coli hisB mutation was determined and an ORF of 624 nucleotides which can code for a protein of 207 amino acids was identified. A significant base sequence homology with the carboxy-terminal moiety of the E. coli hisB gene (0.53) and the Saccharomyces cerevisiae HIS3 gene (0.44), coding for an imidazole glycerolphosphate dehydratase activity was found. The amino acid sequence and composition, the hydropathic profile and the predicted secondary structures of the yeast, E. coli and A. brasilense proteins were compared. The significance of the data presented is discussed
1989
216
224
229
R. Fani; M. Bazzicalupo; G. Damiani; A. Bianchi; C. Schipani; V. Sgaramella; M. Polsinelli
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/11474
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