Structure of the second RRM domain of Nrd1, a fission yeast MAPK target RNA binding protein, and implication for its RNA recognition and regulation
| Autor: | Yutaka Ito, Ayaho Kobayashi, Toshinobu Fujiwara, Ryosuke Satoh, Masaki Mishima, Teppei Kanaba, Reiko Sugiura |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Biophysics RNA-binding protein Biology Biochemistry Structure-Activity Relationship Binding site Molecular Biology Messenger RNA Binding Sites RNA recognition motif RNA RNA-Binding Proteins RNA Fungal Cell Biology Non-coding RNA Cell biology Protein Structure Tertiary Solutions Ribonucleoproteins Structural Homology Protein Schizosaccharomyces pombe Proteins Mitogen-Activated Protein Kinases Small nuclear RNA Binding domain Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 437(1) |
| ISSN: | 1090-2104 |
| Popis: | Negative regulator of differentiation 1 (Nrd1) is known as a negative regulator of sexual differentiation in fission yeast. Recently, it has been revealed that Nrd1 also regulates cytokinesis, in which physical separation of the cell is achieved by a contractile ring comprising many proteins including actin and myosin. Cdc4, a myosin II light chain, is known to be required for cytokinesis. Nrd1 binds and stabilizes Cdc4 mRNA, and thereby suppressing the cytokinesis defects of the cdc4 mutants. Interestingly, Pmk1 MAPK phosphorylates Nrd1, resulting in markedly reduced RNA binding activity. Furthermore, Nrd1 localizes to stress granules in response to various stresses, and Pmk1 phosphorylation enhances the localization. Nrd1 consists of four RRM domains, although the mechanism by which Pmk1 regulates the RNA binding activity of Nrd1 is unknown. In an effort to delineate the relationship between Nrd1 structure and function, we prepared each RNA binding domain of Nrd1 and examined RNA binding to chemically synthesized oligo RNA using NMR. The structure of the second RRM domain of Nrd1 was determined and the RNA binding site on the second RRM domain was mapped by NMR. A plausible mechanism pertaining to the regulation of RNA binding activity by phosphorylation is also discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect