大肠杆菌的K88ab基因编码一种与K88ab菌毛粘附素不同的菌毛样蛋白。
K88ab gene of Escherichia coli encodes a fimbria-like protein distinct from the K88ab fimbrial adhesin.
作者信息
Mooi F R, van Buuren M, Koopman G, Roosendaal B, de Graaf F K
出版信息
J Bacteriol. 1984 Aug;159(2):482-7. doi: 10.1128/jb.159.2.482-487.1984.
Abstract
The K88ab adhesin operon of Escherichia coli encodes for a fimbrial protein (the K88ab adhesin) which is involved in colonization of the porcine intestine. We characterized a structural gene (gene A) which is part of the K88ab adhesin operon and codes for an as yet unidentified polypeptide (pA). A mutation in gene A resulted in accumulation of K88ab adhesin subunits inside the cell. The nucleotide sequence of gene A was determined, and the deduced amino acid sequence suggested that pA is synthesized as a precursor containing a typical N-terminal signal peptide. The molecular weight of pA was calculated to be ca. 17,600. Gene A is preceded by a sequence showing homology with the consensus promoter. Fimbrial subunits from a number of E. coli strains have significant homology at their N- and C-termini. pA also contained some of these conserved sequences and showed a number of other similarities with fimbrial subunits. Therefore, it seems likely that the K88ab adhesin operon codes for a fimbrial subunit (pA) distinct from the K88ab adhesin subunit.
摘要
大肠杆菌的K88ab黏附素操纵子编码一种菌毛蛋白（K88ab黏附素），该蛋白参与猪肠道的定植。我们鉴定了一个结构基因（基因A），它是K88ab黏附素操纵子的一部分，编码一种尚未鉴定的多肽（pA）。基因A中的一个突变导致K88ab黏附素亚基在细胞内积累。测定了基因A的核苷酸序列，推导的氨基酸序列表明pA作为含有典型N端信号肽的前体合成。计算出pA的分子量约为17,600。基因A之前有一个与共有启动子显示同源性的序列。许多大肠杆菌菌株的菌毛亚基在其N端和C端具有显著的同源性。pA也包含其中一些保守序列，并与菌毛亚基表现出许多其他相似性。因此，K88ab黏附素操纵子似乎编码一种与K88ab黏附素亚基不同的菌毛亚基（pA）。
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