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Characterization of inner membrane protein YciB in Escherichia coli : YciB interacts with cell elongation and division proteins
Author(s) -
Li Gaochi,
Badaluddin Noor Afiza,
Kitakawa Madoka
Publication year - 2015
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/1348-0421.12330
Subject(s) - biology , cell division , transmembrane protein , escherichia coli , microbiology and biotechnology , cell envelope , membrane protein , mutant , cell , cell membrane , elongation , vesicle associated membrane protein 8 , inner membrane , bacterial outer membrane , biochemistry , membrane , gene , receptor , materials science , ultimate tensile strength , metallurgy , mitochondrion
The function of inner membrane protein YciB in Escherichia coli has not been identified. In this study, the membrane topology of the protein that contains five transmembrane domains was clarified. YciB was found to interact with various proteins involved in cell elongation and cell division using a bacterial two‐hybrid system. It was also found that the deletion mutant of yciB is susceptible to the low osmolarity. These observations together with previous reports indicate that YciB is involved in synthesis of the cell envelope by interacting with cell elongation and cell division complexes.

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