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2rt3

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Revision as of 09:50, 5 August 2016

Solution structure of the second RRM domain of Nrd1

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).^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jeong HT, Ozoe F, Tanaka K, Nakagawa T, Matsuda H, Kawamukai M. A novel gene, msa1, inhibits sexual differentiation in Schizosaccharomyces pombe. Genetics. 2004 May;167(1):77-91. PMID:15166138
↑ Kobayashi A, Kanaba T, Satoh R, Fujiwara T, Ito Y, Sugiura R, Mishima M. Structure of the second RRM domain of Nrd1, a fission yeast MAPK target RNA binding protein, and implication for its RNA recognition and regulation. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2013.06.008

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rt3"

@@ Line 1: / Line 1: @@
 ==Solution structure of the second RRM domain of Nrd1==
 <StructureSection load='2rt3' size='340' side='right' caption='[[2rt3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2rt3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RT3 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rt3 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt3 OCA], [http://pdbe.org/2rt3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rt3 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2rt3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2rt3

From Proteopedia

Revision as of 09:50, 5 August 2016

Solution structure of the second RRM domain of Nrd1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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