4ll8: Difference between revisions

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==Complex of carboxy terminal domain of Myo4p and She3p middle fragment==
==Complex of carboxy terminal domain of Myo4p and She3p middle fragment==
<StructureSection load='4ll8' size='340' side='right' caption='[[4ll8]], [[Resolution|resolution]] 3.58&Aring;' scene=''>
<StructureSection load='4ll8' size='340' side='right' caption='[[4ll8]], [[Resolution|resolution]] 3.58&Aring;' scene=''>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ll6|4ll6]], [[4ll7|4ll7]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ll6|4ll6]], [[4ll7|4ll7]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO4, SHE1, YAL029C, FUN22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SHE3, YBR130C, YBR1005 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO4, SHE1, YAL029C, FUN22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SHE3, YBR130C, YBR1005 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's 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=4ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll8 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=4ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll8 OCA], [http://pdbe.org/4ll8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4ll8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Revision as of 01:00, 5 August 2016

Complex of carboxy terminal domain of Myo4p and She3p middle fragmentComplex of carboxy terminal domain of Myo4p and She3p middle fragment

Structural highlights

4ll8 is a 3 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:MYO4, SHE1, YAL029C, FUN22 (Baker's yeast), SHE3, YBR130C, YBR1005 (Baker's yeast)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYO4_YEAST] Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruited to specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease, via its interaction with SHE3.[1] [2] [3] [4] [5] [6] [SHE3_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. Required for the delivery of cortical endoplasmic reticulum into the emerging bud.[7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17]

Publication Abstract from PubMed

Myosin 4 protein (Myo4p), one of five distinct myosins of yeast, is dedicated to cytoplasmic transport of two types of cargos, zipcoded messenger ribonucleoprotein particles (mRNPs) and tubular endoplasmic reticulum (tER). Neither cargo binds directly to Myo4p. Instead, swi5p-dependent HO expression 3 protein (She3p) serves as an "adaptor" that contains three binding modules, one for Myo4p and one each for zipcoded mRNP and tER. The assembly of a transport-competent motor complex is poorly understood. Here, we report that Myo4p*She3p forms a stable 1:2 heterotrimer in solution. In the Myo4p*She3p crystal structure, Myo4p's C-terminal domain (CTD) assumes a lobster claw-shaped form, the minor prong of which adheres to a pseudocoiled-coil region of She3p. The extensive Myo4p*She3p interactome buries 3,812 A(2) surface area and is primarily hydrophobic. Because the Myo4p*She3p heterotrimer contains only one myosin molecule, it is not transport-competent. By stepwise reconstitution, we found a single molecule of synthetic oligonucleotide (representing the mRNA zipcode element) bound to a single tetramer of zipcode binding protein She2p to be sufficient for Myo4p*She3p dimerization. Therefore, cargo initiates cross-linking of two Myo4p*She3p heterotrimers to an ensemble that contains two myosin molecules obligatory for movement. An additional crystal structure comprising an overlapping upstream portion of She3p showed continuation of the pseudocoiled-coil structure and revealed another highly conserved surface region. We suggest this region as a candidate binding site for a yet unidentified tER ligand. We propose a model whereby zipcoded mRNP and/or tER ligands couple two Myo4p*She3p heterotrimers and thereby generate a transport-competent motor complex either for separate transport or cotransport of these two cargos.

Structure of a myosin*adaptor complex and pairing by cargo.,Shi H, Singh N, Esselborn F, Blobel G Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):E1082-90. doi:, 10.1073/pnas.1401428111. Epub 2014 Feb 12. PMID:24522109[18]

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

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ Heuck A, Fetka I, Brewer DN, Huls D, Munson M, Jansen RP, Niessing D. The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J Cell Biol. 2010 May 3;189(3):497-510. PMID:20439999 doi:10.1083/jcb.201002076
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ 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
  11. ↑ 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
  12. ↑ 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
  13. ↑ 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
  14. ↑ 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
  15. ↑ 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
  16. ↑ 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
  17. ↑ Landers SM, Gallas MR, Little J, Long RM. She3p possesses a novel activity required for ASH1 mRNA localization in Saccharomyces cerevisiae. Eukaryot Cell. 2009 Jul;8(7):1072-83. Epub 2009 May 8. PMID:19429778 doi:http://dx.doi.org/EC.00084-09
  18. ↑ Shi H, Singh N, Esselborn F, Blobel G. Structure of a myosin*adaptor complex and pairing by cargo. Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):E1082-90. doi:, 10.1073/pnas.1401428111. Epub 2014 Feb 12. PMID:24522109 doi:http://dx.doi.org/10.1073/pnas.1401428111

4ll8, resolution 3.58Å

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