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Biogenesis of membrane bound respiratory complexes in Escherichia coli

Price, C. E. & Driessen, A. J. M., Jun-2010, In : Biochimica et Biophysica Acta-Molecular Cell Research. 1803, 6, p. 748 - 766 19 p.

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  • Biogenesis of membrane bound respiratory complexes

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DOI

Escherichia colt is one of the preferred bacteria for studies on the energetics and regulation of respiration Respiratory chains consist of primary dehydrogenases and terminal reductases or oxidases linked by quinones. In order to assemble this complex arrangement of protein complexes, synthesis of the subunits occurs in the cytoplasm followed by assembly in the cytoplasm and/or membrane, the incorporation of metal or organic cofactors and the anchoring of the complex to the membrane In the case of exported metalloproteins, synthesis, assembly and incorporation of metal cofactors must be completed before translocation across the cytoplasmic membrane Coordination data on these processes is, however, scarce In this review, we discuss the various processes that respiratory proteins must undergo for correct assembly and functional coupling to the electron transport chain in E colt. Targeting to and translocation across the membrane together with cofactor synthesis and insertion are discussed in a general manner followed by a review of the coordinated biogenesis of individual respiratory enzyme complexes. Lastly, we address the supramolecular organization of respiratory enzymes into supercomplexes and their localization to specialized domains in the membrane (C) 2010 Elsevier B V All rights reserved

Original languageEnglish
Pages (from-to)748 - 766
Number of pages19
JournalBiochimica et Biophysica Acta-Molecular Cell Research
Volume1803
Issue number6
Publication statusPublished - Jun-2010

    Keywords

  • YidC, SecYEG, SecA, Tat, Respiration, ATP synthase, NADH-UBIQUINONE OXIDOREDUCTASE, DIMETHYL-SULFOXIDE REDUCTASE, C-TYPE CYTOCHROMES, F1F0 ATP SYNTHASE, TWIN-ARGININE TRANSLOCASE, SEC-INDEPENDENT PROTEIN, PROKARYOTIC NITRATE REDUCTASES, SIGNAL RECOGNITION PARTICLE, DEPENDENT NITRITE REDUCTION, TERMINAL OXIDASE COMPLEX

ID: 1933522