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The membrane insertase YidC.
Dalbey, Ross E; Kuhn, Andreas; Zhu, Lu; Kiefer, Doro.
Affiliation
  • Dalbey RE; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. Electronic address: dalbey@chemistry.ohio-state.edu.
  • Kuhn A; Institute of Microbiology and Molecular Biology, University of Hohenheim, Garbenstr 30, 70599 Stuttgart, Germany. Electronic address: Andreas.Kuhn@uni-hohenheim.de.
  • Zhu L; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
  • Kiefer D; Institute of Microbiology and Molecular Biology, University of Hohenheim, Garbenstr 30, 70599 Stuttgart, Germany.
Biochim Biophys Acta ; 1843(8): 1489-96, 2014 Aug.
Article in En | MEDLINE | ID: mdl-24418623
ABSTRACT
The membrane insertases YidC-Oxa1-Alb3 provide a simple cellular system that catalyzes the transmembrane topology of newly synthesized membrane proteins. The insertases are composed of a single protein with 5 to 6 transmembrane (TM) helices that contact hydrophobic segments of the substrate proteins. Since YidC also cooperates with the Sec translocase it is widely involved in the assembly of many different membrane proteins including proteins that obtain complex membrane topologies. Homologues found in mitochondria (Oxa1) and thylakoids (Alb3) point to a common evolutionary origin and also demonstrate the general importance of this cellular process. This article is part of a Special Issue entitled Protein trafficking and secretion in bacteria. Guest Editors Anastassios Economou and Ross Dalbey.
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Full text: 1 Database: MEDLINE Main subject: Membrane Transport Proteins / Protein Transport / Mitochondrial Proteins / Thylakoid Membrane Proteins Language: En Journal: Biochim Biophys Acta Year: 2014 Type: Article

Full text: 1 Database: MEDLINE Main subject: Membrane Transport Proteins / Protein Transport / Mitochondrial Proteins / Thylakoid Membrane Proteins Language: En Journal: Biochim Biophys Acta Year: 2014 Type: Article