RRC ID 15698
Author Satoh R, Tanaka A, Kita A, Morita T, Matsumura Y, Umeda N, Takada M, Hayashi S, Tani T, Shinmyozu K, Sugiura R.
Title Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast.
Journal PLoS One
Abstract 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.
Volume 7(1)
Pages e29683
Published 2012-1-1
DOI 10.1371/journal.pone.0029683
PII PONE-D-11-16151
PMID 22276125
PMC PMC3261880
MeSH Arsenites / pharmacology Cadmium Chloride / pharmacology Hydrogen Peroxide / pharmacology Potassium Chloride / pharmacology Protein Binding / drug effects RNA, Fungal / metabolism Receptors for Activated C Kinase Receptors, Cell Surface / metabolism Ribonucleoproteins / metabolism* Schizosaccharomyces / drug effects Schizosaccharomyces / metabolism* Schizosaccharomyces pombe Proteins / metabolism* Sodium Compounds / pharmacology Temperature
IF 2.74
Times Cited 13
Yeast HM123