Expression of prokaryotic and eukaryotic cytochromes c in Escherichia coli.
C-type cytochromes from various sources show substantial structural conservation. For the covalent attachment of heme groups to apocytochromes, however, three different enzyme systems have been described so far. We have examined the ability of the heme ligation systems of Escherichia coli and of Saccharomyces cerevisiae to process cytochromes from S. cerevisiae, Paracoccus denitrificans, and Synechocystis sp. PCC 6803. E. coli's maturation system with at least eight different proteins accepted all these cytochromes for heme ligation. The single subunit heme lyase from S. cerevisiae mitochondria, on the other hand, failed to attach heme groups to cytochromes of prokaryotic origin.
Abteilung Biophysik, Universität Osnabrück, Germany.
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D001051:Apoenzymes / Q000096:biosynthesis; D001059:Apoproteins / Q000096:biosynthesis; D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis; D001426:Bacterial Proteins; D001665:Binding Sites; D003574:Cytochrome c Group / Q000096:biosynthesis / Q000235:genetics*; D045304:Cytochromes c; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D015971:Gene Expression Regulation, Enzymologic; D006420:Hemeproteins / Q000096:biosynthesis; D008190:Lyases / Q000096:biosynthesis; D008565:Membrane Proteins / Q000096:biosynthesis; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins
D001051:Apoenzymes; D001059:Apoproteins; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C118373:CcmA protein, bacteria; C492058:CcmC protein, E coli; C116246:CcmC protein, bacteria; C115384:CcmE protein, E coli; D003574:Cytochrome c Group; D029968:Escherichia coli Proteins; D006420:Hemeproteins; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; C032139:iso-2-cytochrome C; D045304:Cytochromes c; D008190:Lyases; C095893:CYT2 protein, S cerevisiae