生物
霍乱弧菌
基因
大肠杆菌
细菌外膜
微生物学
肽序列
核酸序列
突变体
分子生物学
生物化学
遗传学
细菌
作者
Hannu Lå,E. Tapio Palva
标识
DOI:10.1111/j.1365-2958.1993.tb00960.x
摘要
Summary The outer membrane of Vibrio cholerae contains a maltose‐inducible major protein, OmpS (43 kDa), that is common to different isolates. Nucleotide sequence analysis of the corresponding structural gene, ompS, revealed an open reading frame encoding a 412‐amino‐acid polypeptide. The amino acid sequence of OmpS is similar to that of LamB, the Escherichia coli maltoporin, and to ScrY of Klebsilla pneumoniae, although the antigenic determinants of these proteins are different. The cloned ompS gene complemented an ompS mutation of V. cholerae and the corresponding polypeptide could function as a maltoporin in a LamB ‐ mutant of E. coli. The promoter region of ompS is highly homologous to the malK‐lamB promoter of E. coli and the ompS gene is controlled by MalT in E. coli. This indicates that the same kind of regulatory mechanism is used to activate the ompS expression in V. cholerae and malK‐lamB expression in E. coli. An ompS‐lacZ transcriptional fusion was used to demonstrate a dual control in ompS expression; the ompS gene is responsive to the inducers maltose and trehalose but in their absence it is also expressed in response to growth‐phase. These different modes of induction might be of importance during different stages of V. cholerae infection.
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