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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons Ltd
2014
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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. |
format | Online Article Text |
id | pubmed-4158909 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | John Wiley & Sons Ltd |
record_format | MEDLINE/PubMed |
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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