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

TY - JOUR

T1 - A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins

AU - Weiner, Joel H.

AU - Bilous, Peter T.

AU - Shaw, Gillian M.

AU - Lubitz, Shannon P.

AU - Frost, Laura

AU - Thomas, Gavin H.

AU - Cole, Jeff A.

AU - Turner, Raymond J.

N1 - Funding Information: This work was funded by the Medical Research Council of Canada (grant PG11440). G. T. was supported by a United Kingdom Biotechnology and Biological Sciences Research Studentship with British Nuclear Fuels, Public Limited Company.

PY - 1998/4/3

Y1 - 1998/4/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0032478550&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(00)81149-6

DO - 10.1016/S0092-8674(00)81149-6

M3 - Article

C2 - 9546395

AN - SCOPUS:0032478550

SN - 0092-8674

VL - 93

SP - 93

EP - 101

JO - Cell

JF - Cell

IS - 1

ER -