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Translation, Post-Translational Processing, and Mitochondrial Translocation of Yeast Iso-1-Cytochrome c

  • Fred Sherman
Part of the Basic Life Sciences book series (BLSC, volume 40)

Abstract

The complete biosynthesis and assembly of mitochondrial cytochrome c involves a number of steps, including the following: translation of the extramitochondrial precursor, apocytochrome c, on cytosolic ribosomes; excision of the amino-terminal methionine residue which is incorporated during initiation of translation of cytochrome c and of all other proteins; amino-terminal acetylation of vertebrate and plant cytochrome c and of certain mutant forms of yeast iso-1-cytochrome c; trimethylation of lysines 72 and 86 in plant cytochrome c and lysine 72 in fungal cytochrome c; binding of apocytochrome c to, presumably, a specific receptor on the outer mitochondrial membrane; the covalent attachment of protoheme to two cysteinyl residues, forming two thioether bonds; and the concomitant translocation across the outer mitochondrial membrane. These steps are schematically outlined in Fig. 1 for yeast iso-1-cytochrome c. We have been investigating all of these processes with mutant forms of yeast iso-1-cytochrome c and with cis-acting mutations that control these processes.

Keywords

Methionine Aminopeptidase Hairpin Loop Structure Yeast Cytochrome Cyc3 Mutant Penultimate Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Fred Sherman
    • 1
  1. 1.Departments of Biochemistry and BiophysicsUniversity of Rochester Medical SchoolRochesterUSA

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