Journal
FEBS LETTERS
Volume 585, Issue 21, Pages 3415-3419Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.08.042
Keywords
Holocytochrome c synthase; Heme lyase; Cytochrome c; Heme regulatory motif; CP motif
Funding
- Biotechnology and Biological Sciences Research Council [BB/H017887/1]
- Biotechnology and Biological Sciences Research Council [BB/H017887/1] Funding Source: researchfish
- BBSRC [BB/H017887/1] Funding Source: UKRI
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The function of holocytochrome c synthase (HCCS, also called heme lyase) is to attach covalently the heme cofactor to cytochromes c in the mitochondria of animals, fungi and protozoa. Little is known about how the protein functions but CP motifs, commonly found in heme-binding proteins, are present. Here we examine holocytochrome c production by Saccharomyces cerevisiae HCCS in the Escherichia coli cytoplasm with emphasis on the conserved CP motifs long implicated in heme transfer by this enzyme. Unexpectedly, the two motifs, both towards the N-terminus, were not required for activity. Mutations in HCCS on the C-terminal side of the CP motifs, known to cause disease states in humans (microphthalmia with linear skin defects) abolished or drastically attenuated holocytochrome c production. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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