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Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast
Zinc-finger domains are found in many nucleic acid-binding proteins in both prokaryotes and eukaryotes. Proteins carrying zinc-finger domains have important roles in various nuclear transactions, including transcription, mRNA processing and mRNA export; however, for many individual zinc-finger prote...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711435/ https://www.ncbi.nlm.nih.gov/pubmed/23658229 http://dx.doi.org/10.1093/nar/gkt363 |
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author | Sugiyama, Tomoyasu Wanatabe, Nobuyoshi Kitahata, Eri Tani, Tokio Sugioka-Sugiyama, Rie |
author_facet | Sugiyama, Tomoyasu Wanatabe, Nobuyoshi Kitahata, Eri Tani, Tokio Sugioka-Sugiyama, Rie |
author_sort | Sugiyama, Tomoyasu |
collection | PubMed |
description | Zinc-finger domains are found in many nucleic acid-binding proteins in both prokaryotes and eukaryotes. Proteins carrying zinc-finger domains have important roles in various nuclear transactions, including transcription, mRNA processing and mRNA export; however, for many individual zinc-finger proteins in eukaryotes, the exact function of the protein is not fully understood. Here, we report that Red5 is involved in efficient suppression of specific mRNAs during vegetative growth of Schizosaccharomyces pombe. Red5, which contains five C3H1-type zinc-finger domains, localizes to the nucleus where it forms discrete dots. A red5 point mutation, red5-2, results in the upregulation of specific meiotic mRNAs in vegetative mutant red5-2 cells; northern blot data indicated that these meiotic mRNAs in red5-2 cells have elongated poly(A) tails. RNA-fluorescence in situ hybridization results demonstrate that poly(A)(+) RNA species accumulate in the nucleolar regions of red5-deficient cells. Moreover, Red5 genetically interacts with several mRNA export factors. Unexpectedly, three components of the nuclear pore complex also suppress a specific set of meiotic mRNAs. These results indicate that Red5 function is important to meiotic mRNA degradation; they also suggest possible connections among selective mRNA decay, mRNA export and the nuclear pore complex in vegetative fission yeast. |
format | Online Article Text |
id | pubmed-3711435 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-37114352013-07-15 Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast Sugiyama, Tomoyasu Wanatabe, Nobuyoshi Kitahata, Eri Tani, Tokio Sugioka-Sugiyama, Rie Nucleic Acids Res RNA Zinc-finger domains are found in many nucleic acid-binding proteins in both prokaryotes and eukaryotes. Proteins carrying zinc-finger domains have important roles in various nuclear transactions, including transcription, mRNA processing and mRNA export; however, for many individual zinc-finger proteins in eukaryotes, the exact function of the protein is not fully understood. Here, we report that Red5 is involved in efficient suppression of specific mRNAs during vegetative growth of Schizosaccharomyces pombe. Red5, which contains five C3H1-type zinc-finger domains, localizes to the nucleus where it forms discrete dots. A red5 point mutation, red5-2, results in the upregulation of specific meiotic mRNAs in vegetative mutant red5-2 cells; northern blot data indicated that these meiotic mRNAs in red5-2 cells have elongated poly(A) tails. RNA-fluorescence in situ hybridization results demonstrate that poly(A)(+) RNA species accumulate in the nucleolar regions of red5-deficient cells. Moreover, Red5 genetically interacts with several mRNA export factors. Unexpectedly, three components of the nuclear pore complex also suppress a specific set of meiotic mRNAs. These results indicate that Red5 function is important to meiotic mRNA degradation; they also suggest possible connections among selective mRNA decay, mRNA export and the nuclear pore complex in vegetative fission yeast. Oxford University Press 2013-07 2013-05-08 /pmc/articles/PMC3711435/ /pubmed/23658229 http://dx.doi.org/10.1093/nar/gkt363 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | RNA Sugiyama, Tomoyasu Wanatabe, Nobuyoshi Kitahata, Eri Tani, Tokio Sugioka-Sugiyama, Rie Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title_full | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title_fullStr | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title_full_unstemmed | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title_short | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
title_sort | red5 and three nuclear pore components are essential for efficient suppression of specific mrnas during vegetative growth of fission yeast |
topic | RNA |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711435/ https://www.ncbi.nlm.nih.gov/pubmed/23658229 http://dx.doi.org/10.1093/nar/gkt363 |
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