Fani R, Bazzicalupo M, Damiani G, Bianchi A, Schipani C, Sgaramella V, Polsinelli M
Dipartimento di Biologia Animale e Genetica, Università di Firenze, Italy.
Mol Gen Genet. 1989 Apr;216(2-3):224-9. doi: 10.1007/BF00334360.
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.
在一个4.5 kb的DNA片段上鉴定出一组四个巴西固氮螺菌组氨酸生物合成基因hisA、hisB、hisF和hisH,并通过对大肠杆菌突变体的互补分析和核苷酸序列研究了其组织形式。测定了一个互补大肠杆菌hisB突变的1.3 kb片段的核苷酸序列,鉴定出一个624个核苷酸的开放阅读框,其可编码一个207个氨基酸的蛋白质。发现与编码咪唑甘油磷酸脱水酶活性的大肠杆菌hisB基因的羧基末端部分(0.53)和酿酒酵母HIS3基因(0.44)具有显著的碱基序列同源性。比较了酵母、大肠杆菌和巴西固氮螺菌蛋白质的氨基酸序列和组成、亲水性图谱以及预测的二级结构。讨论了所呈现数据的意义。