THE FLAA LOCUS OF BACILLUS-SUBTILIS IS PART OF A LARGE OPERON CODING FOR FLAGELLAR STRUCTURES, MOTILITY FUNCTIONS, AND AN ATPASE-LIKE POLYPEPTIDE

THE FLAA LOCUS OF BACILLUS-SUBTILIS IS PART OF A LARGE OPERON CODING FOR FLAGELLAR STRUCTURES, MOTILITY FUNCTIONS, AND AN ATPASE-LIKE POLYPEPTIDE
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DOI:
10.1128/jb.173.11.3573-3579.1991
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发表时间:
1991-06-01
影响因子:
3.2
通讯作者:
GALIZZI, A
GALIZZI, A
中科院分区:
生物学3区
文献类型:
--
作者:
ALBERTINI, AM;CARAMORI, T;GALIZZI, A

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我们克隆并测序了8.3kb的枯草芽孢杆菌DNA,该DNA对应于鞭毛生物合成、运动和趋化作用的FlaA基因座。DNA序列显示存在10个完整的开放阅读框和2个不完整的开放阅读框。将推导出的氨基酸序列与数据库进行比较,发现其中9个推导产物与大肠杆菌和鼠伤寒沙门氏菌的一些蛋白质相似,这些蛋白质在鞭毛功能中的作用已被直接证明。特别是,序列数据表明,FlaA操纵子编码M-环蛋白、电机开关的组件以及基体杆的远端部分。该基因序列与肠杆菌鞭毛调节子III区的基因序列非常相似。其中一个开放阅读框被翻译成一个与鼠伤寒沙门氏菌FliI有48%氨基酸同源性的蛋白质,与E.coliATP合成酶的β亚基有29%的同源性。
We cloned and sequenced 8.3 kb of Bacillus subtilis DNA corresponding to the flaA locus involved in flagellar biosynthesis, motility, and chemotaxis. The DNA sequence revealed the presence of 10 complete and 2 incomplete open reading frames. Comparison of the deduced amino acid sequences to data banks showed similarities of nine of the deduced products to a number of proteins of Escherichia coli and Salmonella typhimurium for which a role in flagellar functioning has been directly demonstrated. In particular, the sequence data suggest that the flaA operon codes for the M-ring protein, components of the motor switch, and the distal part of the basal-body rod. The gene order is remarkably similar to that described for region III of the enterobacterial flagellar regulon. One of the open reading frames was translated into a protein with 48% amino acid identity to S. typhimurium FliI and 29% identity to the beta-subunit of E. coli ATP synthase.