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| | ==J-domain of Sis1 protein, Hsp40 co-chaperone from Saccharomyces cerevisiae== | | ==J-domain of Sis1 protein, Hsp40 co-chaperone from Saccharomyces cerevisiae== |
| - | <StructureSection load='4rwu' size='340' side='right' caption='[[4rwu]], [[Resolution|resolution]] 1.25Å' scene=''> | + | <StructureSection load='4rwu' size='340' side='right'caption='[[4rwu]], [[Resolution|resolution]] 1.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rwu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2o37 2o37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rwu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2o37 2o37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RWU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c3g|1c3g]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N2879, SIS1, YNL007C ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwu OCA], [https://pdbe.org/4rwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rwu RCSB], [https://www.ebi.ac.uk/pdbsum/4rwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwu ProSAT]</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=4rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwu OCA], [http://pdbe.org/4rwu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwu RCSB], [http://www.ebi.ac.uk/pdbsum/4rwu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SIS1_YEAST SIS1_YEAST]] Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability. | + | [https://www.uniprot.org/uniprot/SIS1_YEAST SIS1_YEAST] Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Craig, E A]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gu, M]] | + | [[Category: Craig EA]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Gu M]] |
| - | [[Category: Structural genomic]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Osipiuk, J]] | + | [[Category: Osipiuk J]] |
| - | [[Category: Sahi, C]] | + | [[Category: Sahi C]] |
| - | [[Category: Zhou, M]] | + | [[Category: Zhou M]] |
| - | [[Category: Apc90055 5]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Cochaperone]]
| + | |
| - | [[Category: Hsp40]]
| + | |
| - | [[Category: J-domain]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
SIS1_YEAST Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability.
Publication Abstract from PubMed
Unlike other Hsp70 molecular chaperones, those of the eukaryotic cytosol have four residues, EEVD, at their C-termini. EEVD(Hsp70) binds adaptor proteins of the Hsp90 chaperone system and mitochondrial membrane preprotein receptors, thereby facilitating processing of Hsp70-bound clients through protein folding and translocation pathways. Among J-protein co-chaperones functioning in these pathways, Sis1 is unique, as it also binds the EEVD(Hsp70) motif. However, little is known about the role of the Sis1:EEVD(Hsp70) interaction. We found that deletion of EEVD(Hsp70) abolished the ability of Sis1, but not the ubiquitous J-protein Ydj1, to partner with Hsp70 in in vitro protein refolding. Sis1 co-chaperone activity with Hsp70EEVD was restored upon substitution of a glutamic acid of the J-domain. Structural analysis revealed that this key glutamic acid, which is not present in Ydj1, forms a salt bridge with an arginine of the immediately adjacent glycine-rich region. Thus, restoration of Sis1 in vitro activity suggests that intramolecular interactions between the J-domain and glycine-rich region control co-chaperone activity, which is optimal only when Sis1 interacts with the EEVD(Hsp70) motif. However, we found that disruption of the Sis1:EEVD(Hsp70) interaction enhances the ability of Sis1 to substitute for Ydj1 in vivo. Our results are consistent with the idea that interaction of Sis1 with EEVD(Hsp70) minimizes transfer of Sis1-bound clients to Hsp70s that are primed for client transfer to folding and translocation pathways by their preassociation with EEVD binding adaptor proteins. These interactions may be one means by which cells triage Ydj1- and Sis1-bound clients to productive and quality control pathways, respectively.
Roles of intramolecular and intermolecular interactions in functional regulation of the Hsp70 J-protein co-chaperone Sis1.,Yu HY, Ziegelhoffer T, Osipiuk J, Ciesielski SJ, Baranowski M, Zhou M, Joachimiak A, Craig EA J Mol Biol. 2015 Apr 10;427(7):1632-43. doi: 10.1016/j.jmb.2015.02.007. Epub 2015, Feb 14. PMID:25687964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu HY, Ziegelhoffer T, Osipiuk J, Ciesielski SJ, Baranowski M, Zhou M, Joachimiak A, Craig EA. Roles of intramolecular and intermolecular interactions in functional regulation of the Hsp70 J-protein co-chaperone Sis1. J Mol Biol. 2015 Apr 10;427(7):1632-43. doi: 10.1016/j.jmb.2015.02.007. Epub 2015, Feb 14. PMID:25687964 doi:http://dx.doi.org/10.1016/j.jmb.2015.02.007
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