A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins

被引:393
作者
Weiner, JH [1 ]
Bilous, PT
Shaw, GM
Lubitz, SP
Frost, L
Thomas, GH
Cole, JA
Turner, RJ
机构
[1] Univ Alberta, Dept Biochem, MRC, Grp Mol Biol Membranes, Edmonton, AB T6G 2H7, Canada
[2] Univ Alberta, Dept Sci Biol, Edmonton, AB T6G 2E1, Canada
[3] Univ Birmingham, Sch Biochem, Birmingham B15 2TT, W Midlands, England
基金
英国医学研究理事会;
关键词
D O I
10.1016/S0092-8674(00)81149-6
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
We report the identification of the proteins encoded by the mttABC operon (formerly yigTUW), which mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine" leader motif. A pleiotropic-negative mutant in mttA prevents the periplasmic localization of twin arginine redox enzymes, including nitrate reductase (NapA) and trimethylamine N-oxide reductase (TorA). The mutation also prevents the correct localization of the integral membrane molybdoenzyme dimethylsulfoxide reductase (DmsABC). The DmsA subunit has a twin arginine leader. Proteins with a Sec-dependent leader or which assemble spontaneously in the membrane are not affected by this mutation. MttA, B, and C are members of a large family of related sequences extending from archaebacteria to higher eukaryotes.
引用
收藏
页码:93 / 101
页数:9
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