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A novel RING finger in the C-terminal domain of the coatomer protein α-COP

The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by ot...

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Autores principales: Kaur, Gurmeet, Subramanian, Srikrishna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678705/
https://www.ncbi.nlm.nih.gov/pubmed/26666296
http://dx.doi.org/10.1186/s13062-015-0099-9
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author Kaur, Gurmeet
Subramanian, Srikrishna
author_facet Kaur, Gurmeet
Subramanian, Srikrishna
author_sort Kaur, Gurmeet
collection PubMed
description The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13062-015-0099-9) contains supplementary material, which is available to authorized users.
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spelling pubmed-46787052015-12-16 A novel RING finger in the C-terminal domain of the coatomer protein α-COP Kaur, Gurmeet Subramanian, Srikrishna Biol Direct Discovery Notes The C-terminal domain of α-COP, an essential subunit of the COPI coatomer complex, is composed of an all α-helical region and a small β-sheet domain. We show that this β-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13062-015-0099-9) contains supplementary material, which is available to authorized users. BioMed Central 2015-12-14 /pmc/articles/PMC4678705/ /pubmed/26666296 http://dx.doi.org/10.1186/s13062-015-0099-9 Text en © Kaur and Subramanian. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Discovery Notes
Kaur, Gurmeet
Subramanian, Srikrishna
A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title_full A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title_fullStr A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title_full_unstemmed A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title_short A novel RING finger in the C-terminal domain of the coatomer protein α-COP
title_sort novel ring finger in the c-terminal domain of the coatomer protein α-cop
topic Discovery Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678705/
https://www.ncbi.nlm.nih.gov/pubmed/26666296
http://dx.doi.org/10.1186/s13062-015-0099-9
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