Investigation of Escherichia coli dimethyl sulfoxide reductase assembly and processing in strains defective for the sec-independent protein translocation system membrane targeting and translocation.

@article{Sambasivarao2001InvestigationOE,
  title={Investigation of Escherichia coli dimethyl sulfoxide reductase assembly and processing in strains defective for the sec-independent protein translocation system membrane targeting and translocation.},
  author={Damaraju Sambasivarao and Heather A. Dawson and Glen Zhang and Gerry Shaw and Jicheng Hu and Joel H. Weiner},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 23},
  pages={20167-74}
}
Dimethyl sulfoxide reductase is a heterotrimeric enzyme (DmsABC) localized to the cytoplasmic surface of the inner membrane. Targeting of the DmsA and DmsB catalytic subunits to the membrane requires the membrane targeting and translocation (Mtt) system. The DmsAB dimer is a member of a family of extrinsic, cytoplasmic facing membrane subunits that require Mtt in order to assemble on the membrane. We show that the MttA(2), MttB, and presumably MttA(1) but not the MttC proteins are required for… CONTINUE READING
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EBEC Short Reports, 11, 266 Me2SO Reductase Assembly and Processing

  • C. Sanders, N. Wethkamp, H. Lill
  • 2000

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