Import of periplasmic bacteriocins targeting the murein

被引:7
作者
Braun, Volkmar [1 ]
Helbig, Stephanie [1 ]
Patzer, Silke I. [1 ]
机构
[1] Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany
关键词
bacteriocin; colicin; murein; periplasm; TonB; M IMMUNITY PROTEIN; COLICIN-M; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; CATALYTIC DOMAIN; PROLYL ISOMERASE; PESTICIN; FKPA; EXPRESSION; TONB;
D O I
10.1042/BST20120175
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Colicins are the only proteins imported by Escherichia coli and thus serve as tools to study the protein import mechanism. Most of the colicins studied degrade DNA, 16S RNA or tRNA in the cytoplasm, or form pores in the cytoplasmic membrane. Two bacteriocins, Cma (colicin M) and Pst (pesticin), affect the murein structure in the periplasm. These two bacteriocins must be imported only across the outer membrane and therefore represent the simplest system for studying protein import. Cma can be reversibly translocated across the outer membrane. Cma and Pst unfold during import. The crystal structure of Pst reveals a phage T4L (T4 lysozyme) fold of the activity domain. Both bacteriocins require energy for import which is translocated from the cytoplasmic membrane into the outer membrane by the Ton system. Cma kills cells only when the periplasmic FkpA PPIase (peptidylprolyl cis-trans isomerase)/chaperone is present.
引用
收藏
页码:1449 / 1455
页数:7
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