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| | ==NMR structure of Ydj1 J-domain, a cytosolic Hsp40 from Saccharomyces cerevisiae== | | ==NMR structure of Ydj1 J-domain, a cytosolic Hsp40 from Saccharomyces cerevisiae== |
| - | <StructureSection load='5vso' size='340' side='right'caption='[[5vso]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5vso' size='340' side='right'caption='[[5vso]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vso]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VSO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YDJ1, MAS5, YNL064C, N2418, YNL2418C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | </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=5vso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vso OCA], [https://pdbe.org/5vso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vso RCSB], [https://www.ebi.ac.uk/pdbsum/5vso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vso 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=5vso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vso OCA], [http://pdbe.org/5vso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vso RCSB], [http://www.ebi.ac.uk/pdbsum/5vso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vso ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAS5_YEAST MAS5_YEAST]] Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.<ref>PMID:11689685</ref> | + | [https://www.uniprot.org/uniprot/MAS5_YEAST MAS5_YEAST] Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.<ref>PMID:11689685</ref> |
| | <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: Large Structures]] |
| - | [[Category: Ciesielski, S J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Cornilescu, G]] | + | [[Category: Ciesielski SJ]] |
| - | [[Category: Craig, E A]] | + | [[Category: Cornilescu G]] |
| - | [[Category: Lee, W]] | + | [[Category: Craig EA]] |
| - | [[Category: Markley, J L]] | + | [[Category: Lee W]] |
| - | [[Category: Schilke, B A]] | + | [[Category: Markley JL]] |
| - | [[Category: Tonelli, M]] | + | [[Category: Schilke BA]] |
| - | [[Category: Ziegelhoffer, T]] | + | [[Category: Tonelli M]] |
| - | [[Category: Chaperone]]
| + | [[Category: Ziegelhoffer T]] |
| - | [[Category: Dnaj]]
| + | |
| - | [[Category: J-domain]]
| + | |
| - | [[Category: J-protein]]
| + | |
| Structural highlights
Function
MAS5_YEAST Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex.[1]
Publication Abstract from PubMed
By binding to a multitude of polypeptide substrates, Hsp70-based molecular chaperone systems perform a range of cellular functions. All J-protein co-chaperones play the essential role, via action of their J-domains, of stimulating the ATPase activity of Hsp70, thereby stabilizing its interaction with substrate. In addition, J-proteins drive the functional diversity of Hsp70 chaperone systems through action of regions outside their J-domains. Targeting to specific locations within a cellular compartment and binding of specific substrates for delivery to Hsp70 have been identified as modes of J-protein specialization. To better understand J-protein specialization, we concentrated on Saccharomyces cerevisiae SIS1, which encodes an essential J-protein of the cytosol/nucleus. We selected suppressors that allowed cells lacking SIS1 to form colonies. Substitutions changing single residues in Ydj1, a J-protein, which, like Sis1, partners with Hsp70 Ssa1, were isolated. These gain-of-function substitutions were located at the end of the J-domain, suggesting that suppression was connected to interaction with its partner Hsp70, rather than substrate binding or subcellular localization. Reasoning that, if YDJ1 suppressors affect Ssa1 function, substitutions in Hsp70 itself might also be able to overcome the cellular requirement for Sis1, we carried out a selection for SSA1 suppressor mutations. Suppressing substitutions were isolated that altered sites in Ssa1 affecting the cycle of substrate interaction. Together, our results point to a third, additional means by which J-proteins can drive Hsp70's ability to function in a wide range of cellular processes-modulating the Hsp70-substrate interaction cycle.
Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.,Schilke BA, Ciesielski SJ, Ziegelhoffer T, Kamiya E, Tonelli M, Lee W, Cornilescu G, Hines JK, Markley JL, Craig EA PLoS Genet. 2017 Oct 30;13(10):e1007084. doi: 10.1371/journal.pgen.1007084., eCollection 2017 Oct. PMID:29084221[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hon T, Lee HC, Hach A, Johnson JL, Craig EA, Erdjument-Bromage H, Tempst P, Zhang L. The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol. 2001 Dec;21(23):7923-32. PMID:11689685 doi:10.1128/MCB.21.23.7923-7932.2001
- ↑ Schilke BA, Ciesielski SJ, Ziegelhoffer T, Kamiya E, Tonelli M, Lee W, Cornilescu G, Hines JK, Markley JL, Craig EA. Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. PLoS Genet. 2017 Oct 30;13(10):e1007084. doi: 10.1371/journal.pgen.1007084., eCollection 2017 Oct. PMID:29084221 doi:http://dx.doi.org/10.1371/journal.pgen.1007084
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