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Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c

Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N-terminus of the apocytochrome polypeptide...

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Detalles Bibliográficos
Autores principales: Zhang, Yulin, Stevens, Julie M., Ferguson, Stuart J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158909/
https://www.ncbi.nlm.nih.gov/pubmed/25084480
http://dx.doi.org/10.1016/j.febslet.2014.07.026
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author Zhang, Yulin
Stevens, Julie M.
Ferguson, Stuart J.
author_facet Zhang, Yulin
Stevens, Julie M.
Ferguson, Stuart J.
author_sort Zhang, Yulin
collection PubMed
description Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N-terminus of the apocytochrome polypeptide are important protein–protein recognition motifs. Here, we explore further the important features of the N-terminal sequence and investigate what variations in the CXXCH residues are productively recognised by HCCS in its substrate.
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spelling pubmed-41589092014-09-17 Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c Zhang, Yulin Stevens, Julie M. Ferguson, Stuart J. FEBS Lett Article Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N-terminus of the apocytochrome polypeptide are important protein–protein recognition motifs. Here, we explore further the important features of the N-terminal sequence and investigate what variations in the CXXCH residues are productively recognised by HCCS in its substrate. John Wiley & Sons Ltd 2014-09-17 /pmc/articles/PMC4158909/ /pubmed/25084480 http://dx.doi.org/10.1016/j.febslet.2014.07.026 Text en © 2014 The Authors https://creativecommons.org/licenses/by/3.0/This work is licensed under a Creative Commons Attribution 3.0 Unported License (https://creativecommons.org/licenses/by/3.0/) .
spellingShingle Article
Zhang, Yulin
Stevens, Julie M.
Ferguson, Stuart J.
Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title_full Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title_fullStr Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title_full_unstemmed Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title_short Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
title_sort substrate recognition of holocytochrome c synthase: n-terminal region and cxxch motif of mitochondrial cytochrome c
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158909/
https://www.ncbi.nlm.nih.gov/pubmed/25084480
http://dx.doi.org/10.1016/j.febslet.2014.07.026
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