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Evolutionary divergence of the nuclear pore complex from fungi to metazoans
Nuclear pore complex (NPC) is the largest multimeric protein assembly of the eukaryotic cell, which mediates the nucleocytoplasmic transport. The constituent proteins of this assembly (nucleoporins) are present in varying copy numbers to give a size from ~ 60 MDa (yeast) to 112 MDa (human) and share...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6371224/ https://www.ncbi.nlm.nih.gov/pubmed/30488506 http://dx.doi.org/10.1002/pro.3558 |
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author | Chopra, Kriti Bawaria, Shrankhla Chauhan, Radha |
author_facet | Chopra, Kriti Bawaria, Shrankhla Chauhan, Radha |
author_sort | Chopra, Kriti |
collection | PubMed |
description | Nuclear pore complex (NPC) is the largest multimeric protein assembly of the eukaryotic cell, which mediates the nucleocytoplasmic transport. The constituent proteins of this assembly (nucleoporins) are present in varying copy numbers to give a size from ~ 60 MDa (yeast) to 112 MDa (human) and share common ancestry with other membrane‐associated complexes such as COPI/COPII and thus share the same structural folds. However, the nucleoporins across species exhibit very low percentage sequence similarity and this reflects in their distinct secondary structure and domain organization. We employed thorough sequence and phylogenetic analysis guided from structure‐based alignments of all the nucleoporins from fungi to metazoans to understand the evolution of NPC. Through evolutionary pressure analysis on various nucleoporins, we deduced that these proteins are under differential selection pressure and hence the homologous interacting partners do not complement each other in the in vitro pull‐down assay. The super tree analysis of all nucleoporins taken together illustrates divergent evolution of nucleoporins and notably, the degree of divergence is more apparent in higher order organisms as compared to lower species. Overall, our results support the hypothesis that the protein–protein interactions in such large multimeric assemblies are species specific in nature and hence their structure and function should also be studied in an organism‐specific manner. |
format | Online Article Text |
id | pubmed-6371224 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-63712242019-02-26 Evolutionary divergence of the nuclear pore complex from fungi to metazoans Chopra, Kriti Bawaria, Shrankhla Chauhan, Radha Protein Sci Full‐Length Papers Nuclear pore complex (NPC) is the largest multimeric protein assembly of the eukaryotic cell, which mediates the nucleocytoplasmic transport. The constituent proteins of this assembly (nucleoporins) are present in varying copy numbers to give a size from ~ 60 MDa (yeast) to 112 MDa (human) and share common ancestry with other membrane‐associated complexes such as COPI/COPII and thus share the same structural folds. However, the nucleoporins across species exhibit very low percentage sequence similarity and this reflects in their distinct secondary structure and domain organization. We employed thorough sequence and phylogenetic analysis guided from structure‐based alignments of all the nucleoporins from fungi to metazoans to understand the evolution of NPC. Through evolutionary pressure analysis on various nucleoporins, we deduced that these proteins are under differential selection pressure and hence the homologous interacting partners do not complement each other in the in vitro pull‐down assay. The super tree analysis of all nucleoporins taken together illustrates divergent evolution of nucleoporins and notably, the degree of divergence is more apparent in higher order organisms as compared to lower species. Overall, our results support the hypothesis that the protein–protein interactions in such large multimeric assemblies are species specific in nature and hence their structure and function should also be studied in an organism‐specific manner. John Wiley & Sons, Inc. 2018-12-24 2019-03 /pmc/articles/PMC6371224/ /pubmed/30488506 http://dx.doi.org/10.1002/pro.3558 Text en © 2018 The Authors. Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Full‐Length Papers Chopra, Kriti Bawaria, Shrankhla Chauhan, Radha Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title | Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title_full | Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title_fullStr | Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title_full_unstemmed | Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title_short | Evolutionary divergence of the nuclear pore complex from fungi to metazoans |
title_sort | evolutionary divergence of the nuclear pore complex from fungi to metazoans |
topic | Full‐Length Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6371224/ https://www.ncbi.nlm.nih.gov/pubmed/30488506 http://dx.doi.org/10.1002/pro.3558 |
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