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| - | '''Unreleased structure''' | |
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| - | The entry 7pze is ON HOLD until Oct 12 2023
| + | ==MademoiseLLE domain 2 of Rrm4 from Ustilago maydis== |
| - | | + | <StructureSection load='7pze' size='340' side='right'caption='[[7pze]], [[Resolution|resolution]] 2.60Å' scene=''> |
| - | Authors: Devans, S., Schott-Verdugo, s., Muentjes, K., Olgeiser, L., Reiners, J., Schmitt, L., Hoeppner, A., Smits, S.H., Gohlke, H., Feldbruegge, M.
| + | == Structural highlights == |
| - | | + | <table><tr><td colspan='2'>[[7pze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ustilago_maydis Ustilago maydis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PZE FirstGlance]. <br> |
| - | Description: MademoiseLLE domain 2 of Rrm4 from Ustilago maydis
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | [[Category: Unreleased Structures]] | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pze OCA], [https://pdbe.org/7pze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pze RCSB], [https://www.ebi.ac.uk/pdbsum/7pze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pze ProSAT]</span></td></tr> |
| - | [[Category: Feldbruegge, M]] | + | </table> |
| - | [[Category: Hoeppner, A]] | + | == Function == |
| - | [[Category: Olgeiser, L]] | + | [https://www.uniprot.org/uniprot/RRM4_USTMA RRM4_USTMA] Key RNA-binding protein involved in the formation of polar-growing hyphae which is essential for infection by the plant pathogen (PubMed:15643068, PubMed:17105762, PubMed:19494833). During filamentation, assembles into particles that shuttle bidirectionally along microtubules to both poles (PubMed:17105762, PubMed:19494833, PubMed:30738139). The RRM4 transport particles are part of the endosomal mRNP transport that regulates polarity of the infectious hyphae by transporting distinct mRNAs encoding, for example, the ubiquitin fusion protein UBI1, the small G protein RHO3, or the septin CDC3, from the nucleus to cell poles (PubMed:17105762, PubMed:19494833, PubMed:22357951, PubMed:24355572, PubMed:25985087, PubMed:30738139). Recognizes a broad spectrum of cargo mRNAs and precisely binds at stop codons, which constitute landmark sites of translation, suggesting an intimate connection of mRNA transport and translation (PubMed:30552148). Binds also to the specific binding motif UAUG of cargo mRNAs via its third RRM (PubMed:30552148). Plus-end-directed KIN3, a kinesin-3 type motor, mediates anterograde transport of RRM4-containing mRNPs whereas split dynein DYM1-DYN2 functions in retrograde movement of mRNPs (PubMed:22357951).<ref>PMID:15643068</ref> <ref>PMID:17105762</ref> <ref>PMID:19494833</ref> <ref>PMID:22357951</ref> <ref>PMID:24355572</ref> <ref>PMID:25985087</ref> <ref>PMID:30552148</ref> <ref>PMID:30738139</ref> |
| - | [[Category: Devans, S]] | + | == References == |
| - | [[Category: Smits, S.H]] | + | <references/> |
| - | [[Category: Gohlke, H]] | + | __TOC__ |
| - | [[Category: Reiners, J]] | + | </StructureSection> |
| - | [[Category: Muentjes, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Schott-Verdugo, S]] | + | [[Category: Ustilago maydis]] |
| - | [[Category: Schmitt, L]] | + | [[Category: Devans S]] |
| | + | [[Category: Feldbruegge M]] |
| | + | [[Category: Gohlke H]] |
| | + | [[Category: Hoeppner A]] |
| | + | [[Category: Muentjes K]] |
| | + | [[Category: Olgeiser L]] |
| | + | [[Category: Reiners J]] |
| | + | [[Category: Schmitt L]] |
| | + | [[Category: Schott-Verdugo s]] |
| | + | [[Category: Smits SH]] |
| Structural highlights
Function
RRM4_USTMA Key RNA-binding protein involved in the formation of polar-growing hyphae which is essential for infection by the plant pathogen (PubMed:15643068, PubMed:17105762, PubMed:19494833). During filamentation, assembles into particles that shuttle bidirectionally along microtubules to both poles (PubMed:17105762, PubMed:19494833, PubMed:30738139). The RRM4 transport particles are part of the endosomal mRNP transport that regulates polarity of the infectious hyphae by transporting distinct mRNAs encoding, for example, the ubiquitin fusion protein UBI1, the small G protein RHO3, or the septin CDC3, from the nucleus to cell poles (PubMed:17105762, PubMed:19494833, PubMed:22357951, PubMed:24355572, PubMed:25985087, PubMed:30738139). Recognizes a broad spectrum of cargo mRNAs and precisely binds at stop codons, which constitute landmark sites of translation, suggesting an intimate connection of mRNA transport and translation (PubMed:30552148). Binds also to the specific binding motif UAUG of cargo mRNAs via its third RRM (PubMed:30552148). Plus-end-directed KIN3, a kinesin-3 type motor, mediates anterograde transport of RRM4-containing mRNPs whereas split dynein DYM1-DYN2 functions in retrograde movement of mRNPs (PubMed:22357951).[1] [2] [3] [4] [5] [6] [7] [8]
References
- ↑ Becht P, Vollmeister E, Feldbrugge M. Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis. Eukaryot Cell. 2005 Jan;4(1):121-33. doi: 10.1128/EC.4.1.121-133.2005. PMID:15643068 doi:http://dx.doi.org/10.1128/EC.4.1.121-133.2005
- ↑ Becht P, Konig J, Feldbrugge M. The RNA-binding protein Rrm4 is essential for polarity in Ustilago maydis and shuttles along microtubules. J Cell Sci. 2006 Dec 1;119(Pt 23):4964-73. doi: 10.1242/jcs.03287. Epub 2006 Nov , 14. PMID:17105762 doi:http://dx.doi.org/10.1242/jcs.03287
- ↑ Konig J, Baumann S, Koepke J, Pohlmann T, Zarnack K, Feldbrugge M. The fungal RNA-binding protein Rrm4 mediates long-distance transport of ubi1 and rho3 mRNAs. EMBO J. 2009 Jul 8;28(13):1855-66. doi: 10.1038/emboj.2009.145. Epub 2009 Jun 4. PMID:19494833 doi:http://dx.doi.org/10.1038/emboj.2009.145
- ↑ Baumann S, Pohlmann T, Jungbluth M, Brachmann A, Feldbrugge M. Kinesin-3 and dynein mediate microtubule-dependent co-transport of mRNPs and endosomes. J Cell Sci. 2012 Jun 1;125(Pt 11):2740-52. doi: 10.1242/jcs.101212. Epub 2012 Feb , 22. PMID:22357951 doi:http://dx.doi.org/10.1242/jcs.101212
- ↑ Baumann S, Konig J, Koepke J, Feldbrugge M. Endosomal transport of septin mRNA and protein indicates local translation on endosomes and is required for correct septin filamentation. EMBO Rep. 2014 Jan;15(1):94-102. doi: 10.1002/embr.201338037. Epub 2013 Dec 15. PMID:24355572 doi:http://dx.doi.org/10.1002/embr.201338037
- ↑ Pohlmann T, Baumann S, Haag C, Albrecht M, Feldbrugge M. A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking. Elife. 2015 May 18;4. doi: 10.7554/eLife.06041. PMID:25985087 doi:http://dx.doi.org/10.7554/eLife.06041
- ↑ Olgeiser L, Haag C, Boerner S, Ule J, Busch A, Koepke J, Konig J, Feldbrugge M, Zarnack K. The key protein of endosomal mRNP transport Rrm4 binds translational landmark sites of cargo mRNAs. EMBO Rep. 2019 Jan;20(1):e46588. doi: 10.15252/embr.201846588. Epub 2018 Dec 14. PMID:30552148 doi:http://dx.doi.org/10.15252/embr.201846588
- ↑ Muller J, Pohlmann T, Feldbrugge M. Core components of endosomal mRNA transport are evolutionarily conserved in fungi. Fungal Genet Biol. 2019 May;126:12-16. doi: 10.1016/j.fgb.2019.01.013. Epub 2019 , Feb 6. PMID:30738139 doi:http://dx.doi.org/10.1016/j.fgb.2019.01.013
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