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- | [[Image:1xly.gif|left|200px]]<br /><applet load="1xly" size="450" color="white" frame="true" align="right" spinBox="true" | |
- | caption="1xly, resolution 1.95Å" /> | |
- | '''X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p'''<br /> | |
| | | |
- | ==Overview== | + | ==X-RAY STRUCTURE OF THE RNA-BINDING PROTEIN SHE2p== |
- | Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures, asymmetric distribution of information within and among eukaryotic cells., Actin-dependent transport of ASH1 mRNA in yeast represents one of the, best-characterized examples of mRNP translocation. Formation of the ASH1, mRNP requires recognition of zip code elements by the RNA binding protein, She2p. We determined the X-ray structure of She2p at 1.95 A resolution., She2p is a member of a previously unknown class of nucleic acid binding, proteins, composed of a single globular domain with a five alpha helix, bundle that forms a symmetric homodimer. After demonstrating potent, dimer-dependent RNA binding in vitro, we mapped the RNA binding surface of, She2p to a basic helical hairpin in vitro and in vivo and present a, mechanism for mRNA-dependent initiation of ASH1 mRNP complex assembly.
| + | <StructureSection load='1xly' size='340' side='right'caption='[[1xly]], [[Resolution|resolution]] 1.95Å' scene=''> |
- | | + | == Structural highlights == |
- | ==About this Structure== | + | <table><tr><td colspan='2'>[[1xly]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLY FirstGlance]. <br> |
- | 1XLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XLY OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
- | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xly OCA], [https://pdbe.org/1xly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xly RCSB], [https://www.ebi.ac.uk/pdbsum/1xly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xly ProSAT]</span></td></tr> |
- | ==Reference== | + | </table> |
- | She2p is a novel RNA binding protein with a basic helical hairpin motif., Niessing D, Huttelmaier S, Zenklusen D, Singer RH, Burley SK, Cell. 2004 Nov 12;119(4):491-502. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15537539 15537539]
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/SHE2_YEAST SHE2_YEAST] RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruites also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA.<ref>PMID:10212145</ref> <ref>PMID:10359695</ref> <ref>PMID:11032818</ref> <ref>PMID:11101531</ref> <ref>PMID:12499354</ref> <ref>PMID:13679573</ref> <ref>PMID:14561888</ref> <ref>PMID:14691136</ref> <ref>PMID:15328357</ref> <ref>PMID:15537539</ref> <ref>PMID:15899876</ref> <ref>PMID:16890529</ref> <ref>PMID:18566598</ref> <ref>PMID:19244342</ref> <ref>PMID:20713510</ref> <ref>PMID:9809065</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/1xly_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xly ConSurf]. |
| + | <div style="clear:both"></div> |
| + | == References == |
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Single protein]]
| + | [[Category: Burley SK]] |
- | [[Category: Burley, S.K.]] | + | [[Category: Huettelmaier S]] |
- | [[Category: Huettelmaier, S.]] | + | [[Category: Niessing D]] |
- | [[Category: Niessing, D.]] | + | [[Category: Singer RH]] |
- | [[Category: Singer, R.H.]] | + | [[Category: Zenklusen D]] |
- | [[Category: Zenklusen, D.]] | + | |
- | [[Category: basic helical hairpin]]
| + | |
- | [[Category: dimer]]
| + | |
- | [[Category: five helix bundle]]
| + | |
- | [[Category: rna-binding protein]]
| + | |
- | | + | |
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:09:59 2007''
| + | |
| Structural highlights
Function
SHE2_YEAST RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruites also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Munchow S, Sauter C, Jansen RP. Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins. J Cell Sci. 1999 May;112 ( Pt 10):1511-8. PMID:10212145
- ↑ Beach DL, Salmon ED, Bloom K. Localization and anchoring of mRNA in budding yeast. Curr Biol. 1999 Jun 3;9(11):569-78. PMID:10359695
- ↑ Bohl F, Kruse C, Frank A, Ferring D, Jansen RP. She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p. EMBO J. 2000 Oct 16;19(20):5514-24. PMID:11032818 doi:http://dx.doi.org/10.1093/emboj/19.20.5514
- ↑ Long RM, Gu W, Lorimer E, Singer RH, Chartrand P. She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. EMBO J. 2000 Dec 1;19(23):6592-601. PMID:11101531 doi:http://dx.doi.org/10.1093/emboj/19.23.6592
- ↑ Kruse C, Jaedicke A, Beaudouin J, Bohl F, Ferring D, Guttler T, Ellenberg J, Jansen RP. Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p. J Cell Biol. 2002 Dec 23;159(6):971-82. Epub 2002 Dec 23. PMID:12499354 doi:http://dx.doi.org/10.1083/jcb.200207101
- ↑ Shepard KA, Gerber AP, Jambhekar A, Takizawa PA, Brown PO, Herschlag D, DeRisi JL, Vale RD. Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-localized transcripts using DNA microarray analysis. Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11429-34. Epub 2003 Sep 17. PMID:13679573 doi:http://dx.doi.org/10.1073/pnas.2033246100
- ↑ Gonsalvez GB, Lehmann KA, Ho DK, Stanitsa ES, Williamson JR, Long RM. RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex. RNA. 2003 Nov;9(11):1383-99. PMID:14561888
- ↑ Estrada P, Kim J, Coleman J, Walker L, Dunn B, Takizawa P, Novick P, Ferro-Novick S. Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae. J Cell Biol. 2003 Dec 22;163(6):1255-66. PMID:14691136 doi:http://dx.doi.org/10.1083/jcb.200304030
- ↑ Gonsalvez GB, Little JL, Long RM. ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex. J Biol Chem. 2004 Oct 29;279(44):46286-94. Epub 2004 Aug 23. PMID:15328357 doi:http://dx.doi.org/10.1074/jbc.M406086200
- ↑ Niessing D, Huttelmaier S, Zenklusen D, Singer RH, Burley SK. She2p is a novel RNA binding protein with a basic helical hairpin motif. Cell. 2004 Nov 12;119(4):491-502. PMID:15537539 doi:10.1016/j.cell.2004.10.018
- ↑ Olivier C, Poirier G, Gendron P, Boisgontier A, Major F, Chartrand P. Identification of a conserved RNA motif essential for She2p recognition and mRNA localization to the yeast bud. Mol Cell Biol. 2005 Jun;25(11):4752-66. PMID:15899876 doi:http://dx.doi.org/10.1128/MCB.25.11.4752-4766.2005
- ↑ Schmid M, Jaedicke A, Du TG, Jansen RP. Coordination of endoplasmic reticulum and mRNA localization to the yeast bud. Curr Biol. 2006 Aug 8;16(15):1538-43. PMID:16890529 doi:http://dx.doi.org/10.1016/j.cub.2006.06.025
- ↑ Du TG, Jellbauer S, Muller M, Schmid M, Niessing D, Jansen RP. Nuclear transit of the RNA-binding protein She2 is required for translational control of localized ASH1 mRNA. EMBO Rep. 2008 Aug;9(8):781-7. doi: 10.1038/embor.2008.112. Epub 2008 Jun 20. PMID:18566598 doi:http://dx.doi.org/10.1038/embor.2008.112
- ↑ Shen Z, Paquin N, Forget A, Chartrand P. Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p. Mol Biol Cell. 2009 Apr;20(8):2265-75. doi: 10.1091/mbc.E08-11-1151. Epub 2009, Feb 25. PMID:19244342 doi:http://dx.doi.org/10.1091/mbc.E08-11-1151
- ↑ Shen Z, St-Denis A, Chartrand P. Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud. Genes Dev. 2010 Sep 1;24(17):1914-26. doi: 10.1101/gad.1937510. Epub 2010 Aug 16. PMID:20713510 doi:http://dx.doi.org/10.1101/gad.1937510
- ↑ Bertrand E, Chartrand P, Schaefer M, Shenoy SM, Singer RH, Long RM. Localization of ASH1 mRNA particles in living yeast. Mol Cell. 1998 Oct;2(4):437-45. PMID:9809065
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