Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast.
We have previously identified the RNA recognition motif (RRM)-type RNA-binding protein Nrd1 as an important regulator of the posttranscriptional expression of myosin in fission yeast. Pmk1 MAPK-dependent phosphorylation negatively regulates the RNA-binding activity of Nrd1. Here, we report the role...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3261880?pdf=render |
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| author | Ryosuke Satoh Akitomo Tanaka Ayako Kita Takahiro Morita Yasuhiro Matsumura Nanae Umeda Makoto Takada Sachiko Hayashi Tokio Tani Kaori Shinmyozu Reiko Sugiura |
| author_facet | Ryosuke Satoh Akitomo Tanaka Ayako Kita Takahiro Morita Yasuhiro Matsumura Nanae Umeda Makoto Takada Sachiko Hayashi Tokio Tani Kaori Shinmyozu Reiko Sugiura |
| author_sort | Ryosuke Satoh |
| collection | DOAJ |
| description | We have previously identified the RNA recognition motif (RRM)-type RNA-binding protein Nrd1 as an important regulator of the posttranscriptional expression of myosin in fission yeast. Pmk1 MAPK-dependent phosphorylation negatively regulates the RNA-binding activity of Nrd1. Here, we report the role of Nrd1 in stress-induced RNA granules. Nrd1 can localize to poly(A)-binding protein (Pabp)-positive RNA granules in response to various stress stimuli, including heat shock, arsenite treatment, and oxidative stress. Interestingly, compared with the unphosphorylatable Nrd1, Nrd1(DD) (phosphorylation-mimic version of Nrd1) translocates more quickly from the cytoplasm to the stress granules in response to various stimuli; this suggests that the phosphorylation of Nrd1 by MAPK enhances its localization to stress-induced cytoplasmic granules. Nrd1 binds to Cpc2 (fission yeast RACK) in a phosphorylation-dependent manner and deletion of Cpc2 affects the formation of Nrd1-positive granules upon arsenite treatment. Moreover, the depletion of Nrd1 leads to a delay in Pabp-positive RNA granule formation, and overexpression of Nrd1 results in an increased size and number of Pabp-positive granules. Interestingly, Nrd1 deletion induced resistance to sustained stresses and enhanced sensitivity to transient stresses. In conclusion, our results indicate that Nrd1 plays a role in stress-induced granule formation, which affects stress resistance in fission yeast. |
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| id | doaj.art-a530408533ed460d8e1cd3c86bb708b1 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-14T06:00:08Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
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| series | PLoS ONE |
| spelling | doaj.art-a530408533ed460d8e1cd3c86bb708b12022-12-22T02:08:47ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0171e2968310.1371/journal.pone.0029683Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast.Ryosuke SatohAkitomo TanakaAyako KitaTakahiro MoritaYasuhiro MatsumuraNanae UmedaMakoto TakadaSachiko HayashiTokio TaniKaori ShinmyozuReiko SugiuraWe have previously identified the RNA recognition motif (RRM)-type RNA-binding protein Nrd1 as an important regulator of the posttranscriptional expression of myosin in fission yeast. Pmk1 MAPK-dependent phosphorylation negatively regulates the RNA-binding activity of Nrd1. Here, we report the role of Nrd1 in stress-induced RNA granules. Nrd1 can localize to poly(A)-binding protein (Pabp)-positive RNA granules in response to various stress stimuli, including heat shock, arsenite treatment, and oxidative stress. Interestingly, compared with the unphosphorylatable Nrd1, Nrd1(DD) (phosphorylation-mimic version of Nrd1) translocates more quickly from the cytoplasm to the stress granules in response to various stimuli; this suggests that the phosphorylation of Nrd1 by MAPK enhances its localization to stress-induced cytoplasmic granules. Nrd1 binds to Cpc2 (fission yeast RACK) in a phosphorylation-dependent manner and deletion of Cpc2 affects the formation of Nrd1-positive granules upon arsenite treatment. Moreover, the depletion of Nrd1 leads to a delay in Pabp-positive RNA granule formation, and overexpression of Nrd1 results in an increased size and number of Pabp-positive granules. Interestingly, Nrd1 deletion induced resistance to sustained stresses and enhanced sensitivity to transient stresses. In conclusion, our results indicate that Nrd1 plays a role in stress-induced granule formation, which affects stress resistance in fission yeast.http://europepmc.org/articles/PMC3261880?pdf=render |
| spellingShingle | Ryosuke Satoh Akitomo Tanaka Ayako Kita Takahiro Morita Yasuhiro Matsumura Nanae Umeda Makoto Takada Sachiko Hayashi Tokio Tani Kaori Shinmyozu Reiko Sugiura Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. PLoS ONE |
| title | Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. |
| title_full | Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. |
| title_fullStr | Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. |
| title_full_unstemmed | Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. |
| title_short | Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast. |
| title_sort | role of the rna binding protein nrd1 in stress granule formation and its implication in the stress response in fission yeast |
| url | http://europepmc.org/articles/PMC3261880?pdf=render |
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