PMID:9546395
| Citation |
Weiner, JH, Bilous, PT, Shaw, GM, Lubitz, SP, Frost, L, Thomas, GH, Cole, JA and Turner, RJ (1998) A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93:93-101 |
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| Abstract |
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. |
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| Keywords |
2S Albumins, Plant; Amino Acid Sequence; Arginine/metabolism; Cell Membrane/enzymology; Cloning, Molecular; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Genotype; Iron-Sulfur Proteins; Kinetics; Membrane Proteins/biosynthesis; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Transport Proteins; Molecular Sequence Data; NADH, NADPH Oxidoreductases/metabolism; Nitrate Reductase; Nitrate Reductases/metabolism; Operon; Oxidoreductases/metabolism; Oxidoreductases Acting on CH-NH Group Donors; Plant Proteins/metabolism; Plasmids; Polymerase Chain Reaction; Protein Sorting Signals/chemistry; Protein Structure, Secondary; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Sequence Alignment |
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