2rt3 | pdb_00002rt3

Solution structure of the second RRM domain of Nrd1

spinqualitylabelsall models 2rt3, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rt3 is a 1 chain structure with sequence from Fission yeast. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: nrd1 (Fission yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NRD1_SCHPO] Negative regulator of sexual differentiation. Acts by repressing the transcription of meiosis-inducing, ste11-regulated genes until cells reach a critical level of starvation. RNA-binding protein that preferentially binds poly(U). Publication Abstract from PubMed 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. Structure of the second RRM domain of Nrd1, a fission yeast MAPK target RNA binding protein, and implication for its RNA recognition and regulation.,Kobayashi A, Kanaba T, Satoh R, Fujiwara T, Ito Y, Sugiura R, Mishima M Biochem Biophys Res Commun. 2013 Jul 19;437(1):12-7. doi:, 10.1016/j.bbrc.2013.06.008. Epub 2013 Jun 12. PMID:23770370 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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