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PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline
PUF family proteins are well-conserved regulators of cell proliferation in different developmental processes. They regulate target mRNAs by promoting degradation or by influencing translation through interaction with the translation initiation machinery. Here we show that Caenorhabditis elegans PUF-...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Company of Biologists
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585663/ https://www.ncbi.nlm.nih.gov/pubmed/23444359 http://dx.doi.org/10.1242/dev.087833 |
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author | Pushpa, Kumari Kumar, Ganga Anil Subramaniam, Kuppuswamy |
author_facet | Pushpa, Kumari Kumar, Ganga Anil Subramaniam, Kuppuswamy |
author_sort | Pushpa, Kumari |
collection | PubMed |
description | PUF family proteins are well-conserved regulators of cell proliferation in different developmental processes. They regulate target mRNAs by promoting degradation or by influencing translation through interaction with the translation initiation machinery. Here we show that Caenorhabditis elegans PUF-8 functions redundantly with the nuclear protein TCER-1 in the post-transcriptional maintenance of at least six germline mRNAs. The levels of spliced mRNAs in the puf-8(-) tcer-1(-) double mutant are only 10-30% of the wild type, whereas the unspliced forms increase by ∼2- to 3-fold compared with the wild type. These two proteins colocalise at the inner nuclear periphery, and their absence leads to reduced germ cell proliferation and to sterility. A yeast two-hybrid screen of 31 components of the nuclear pore complex and mRNA processing machineries identified seven proteins involved in mRNA export as potential partners of PUF-8. One of these, the nuclear cap-binding protein NCBP-2, colocalises with PUF-8 in the nucleus. A 50 amino acid N-terminal domain of PUF-8 is essential for interaction with NCBP-2 and for PUF-8 to function redundantly with TCER-1. These results reveal two important unexpected aspects of PUF proteins: that, in addition to the C-terminal PUF domain, the N-terminal domain is crucial for PUF function, and that PUF proteins have a novel role in mRNA maintenance. We propose that PUF proteins, in addition to their known cytoplasmic roles, participate in nuclear processing and/or export of mRNAs. |
format | Online Article Text |
id | pubmed-3585663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-35856632013-03-15 PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline Pushpa, Kumari Kumar, Ganga Anil Subramaniam, Kuppuswamy Development Research Articles PUF family proteins are well-conserved regulators of cell proliferation in different developmental processes. They regulate target mRNAs by promoting degradation or by influencing translation through interaction with the translation initiation machinery. Here we show that Caenorhabditis elegans PUF-8 functions redundantly with the nuclear protein TCER-1 in the post-transcriptional maintenance of at least six germline mRNAs. The levels of spliced mRNAs in the puf-8(-) tcer-1(-) double mutant are only 10-30% of the wild type, whereas the unspliced forms increase by ∼2- to 3-fold compared with the wild type. These two proteins colocalise at the inner nuclear periphery, and their absence leads to reduced germ cell proliferation and to sterility. A yeast two-hybrid screen of 31 components of the nuclear pore complex and mRNA processing machineries identified seven proteins involved in mRNA export as potential partners of PUF-8. One of these, the nuclear cap-binding protein NCBP-2, colocalises with PUF-8 in the nucleus. A 50 amino acid N-terminal domain of PUF-8 is essential for interaction with NCBP-2 and for PUF-8 to function redundantly with TCER-1. These results reveal two important unexpected aspects of PUF proteins: that, in addition to the C-terminal PUF domain, the N-terminal domain is crucial for PUF function, and that PUF proteins have a novel role in mRNA maintenance. We propose that PUF proteins, in addition to their known cytoplasmic roles, participate in nuclear processing and/or export of mRNAs. Company of Biologists 2013-03-15 /pmc/articles/PMC3585663/ /pubmed/23444359 http://dx.doi.org/10.1242/dev.087833 Text en © 2013. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by-nc-sa/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License (http://creativecommons.org/licenses/by-nc-sa/3.0), which permits unrestricted non-commercial use, distribution and reproduction in any medium provided that the original work is properly cited and all further distributions of the work or adaptation are subject to the same Creative Commons License terms. |
spellingShingle | Research Articles Pushpa, Kumari Kumar, Ganga Anil Subramaniam, Kuppuswamy PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title | PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title_full | PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title_fullStr | PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title_full_unstemmed | PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title_short | PUF-8 and TCER-1 are essential for normal levels of multiple mRNAs in the C. elegans germline |
title_sort | puf-8 and tcer-1 are essential for normal levels of multiple mrnas in the c. elegans germline |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585663/ https://www.ncbi.nlm.nih.gov/pubmed/23444359 http://dx.doi.org/10.1242/dev.087833 |
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