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| | ==Solution structure of the C-terminal Pdr1-activating domain of the J-protein Zuo1== | | ==Solution structure of the C-terminal Pdr1-activating domain of the J-protein Zuo1== |
| - | <StructureSection load='2lwx' size='340' side='right'caption='[[2lwx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lwx' size='340' side='right'caption='[[2lwx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lwx]] is a 1 chain structure with sequence from [https://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=2LWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LWX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lwx]] 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=2LWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LWX FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YGR285C, ZUO1 ([https://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=2lwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lwx OCA], [https://pdbe.org/2lwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lwx RCSB], [https://www.ebi.ac.uk/pdbsum/2lwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lwx ProSAT]</span></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=2lwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lwx OCA], [https://pdbe.org/2lwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lwx RCSB], [https://www.ebi.ac.uk/pdbsum/2lwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lwx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ZUO1_YEAST ZUO1_YEAST]] Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.<ref>PMID:15456889</ref> <ref>PMID:15908962</ref>
| + | [https://www.uniprot.org/uniprot/ZUO1_YEAST ZUO1_YEAST] Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.<ref>PMID:15456889</ref> <ref>PMID:15908962</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: Craig, E A]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Ducett, J K]] | + | [[Category: Craig EA]] |
| - | [[Category: Peterson, F C]] | + | [[Category: Ducett JK]] |
| - | [[Category: Volkman, B F]] | + | [[Category: Peterson FC]] |
| - | [[Category: Chaperone]] | + | [[Category: Volkman BF]] |
| - | [[Category: J-protein]]
| + | |
| - | [[Category: Molecular chaperone]]
| + | |
| - | [[Category: Pleiotropic drug resistance]]
| + | |
| Structural highlights
Function
ZUO1_YEAST Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.[1] [2]
Publication Abstract from PubMed
The C-terminal 69 residues of the J-protein Zuo1 are sufficient to activate Pdr1, a transcription factor involved in both pleiotropic drug resistance and growth control. Little is understood about the pathway of activation by this primarily ribosome associated Hsp40 co-chaperone. Here, we report that only the C-terminal 13 residues of Zuo1 are required for activation of Pdr1, with hydrophobic residues being critical for activity. Two-hybrid interaction experiments suggest that the interaction between this 13-residue Zuo1 peptide and Pdr1 is direct, analogous to the activation of Pdr1 by xenobiotics. However, simply dissociation of Zuo1 from the ribosome is not sufficient for induction of Pdr1 transcriptional activity, as the C-terminal 86 residues of Zuo1 fold into an autoinhibitory left-handed four-helix bundle. Hydrophobic residues critical for interaction with Pdr1 are sequestered within the structure of this C-terminal domain (CTD), necessitating unfolding for activation. Thus, although expression of the CTD does not result in activation, alterations that destabilize the structure cause induction of pleiotropic drug resistance. These destabilizing alterations also result in dissociation of the full-length protein from the ribosome. Thus, our results are consistent with an activation pathway in which unfolding of Zuo1's C-terminal helical bundle domain results in ribosome dissociation followed by activation of Pdr1 via a direct interaction.
Unfolding of the C-Terminal Domain of the J-Protein Zuo1 Releases Autoinhibition and Activates Pdr1-Dependent Transcription.,Ducett JK, Peterson FC, Hoover LA, Prunuske AJ, Volkman BF, Craig EA J Mol Biol. 2012 Oct 2. pii: S0022-2836(12)00785-1. doi:, 10.1016/j.jmb.2012.09.020. PMID:23036859[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rakwalska M, Rospert S. The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol Cell Biol. 2004 Oct;24(20):9186-97. PMID:15456889 doi:http://dx.doi.org/10.1128/MCB.24.20.9186-9197.2004
- ↑ Huang P, Gautschi M, Walter W, Rospert S, Craig EA. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol. 2005 Jun;12(6):497-504. Epub 2005 May 22. PMID:15908962 doi:http://dx.doi.org/10.1038/nsmb942
- ↑ Ducett JK, Peterson FC, Hoover LA, Prunuske AJ, Volkman BF, Craig EA. Unfolding of the C-Terminal Domain of the J-Protein Zuo1 Releases Autoinhibition and Activates Pdr1-Dependent Transcription. J Mol Biol. 2012 Oct 2. pii: S0022-2836(12)00785-1. doi:, 10.1016/j.jmb.2012.09.020. PMID:23036859 doi:http://dx.doi.org/10.1016/j.jmb.2012.09.020
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