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6cgh

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Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)

Structural highlights

6cgh is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNJC2_HUMAN Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The J-domain protein Zuotin is a multi-domain eukaryotic Hsp70 co-chaperone. Though it is primarily ribosome-associated, positioned at the exit of the 60S subunit tunnel where it promotes folding of nascent polypeptide chains, Zuotin also has off-ribosome functions. Domains of Zuotin needed for 60S association and interaction with Hsp70 are conserved in eukaryotes. However, whether the 4-helix bundle (4HB) domain is conserved remains an open question. We undertook evolutionary and structural approaches to clarify this issue. We found that the 4HB segment of human Zuotin also forms a bundle of 4 helices. The positive charge of Helix I, which in Saccharomyces cerevisiae is responsible for interaction with the 40S subunit, is particularly conserved. However, the C-termini of fungal and human 4HBs are not similar. In fungi the C-terminal segment forms a plug that folds back into the bundle; in S. cerevisiae it plays an important role in bundle stability and, off the ribosome, in transcriptional activation. In human, C-terminal helix IV of the 4HB is extended, protruding from the bundle. This extension serves as a linker to the regulatory SANT domains, which are present in animals, plants and protists, but not fungi. Further analysis of Zuotin sequences revealed that the plug likely arose as a result of genomic rearrangement upon SANT domain loss early in the fungal lineage. In the lineage leading to S. cerevisiae, the 4HB was subjected to positive selection with the plug becoming increasingly hydrophobic. Eventually, these hydrophobic plug residues were coopted for a novel regulatory function-activation of a recently emerged transcription factor, Pdr1. Our data suggests that Zuotin evolved off-ribosome functions twice-once involving SANT domains, then later in fungi, after SANT domain loss, by coopting the hydrophobic plug. Zuotin serves as an example of complex intertwining of molecular chaperone function and cell regulation.

Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.,Shrestha OK, Sharma R, Tomiczek B, Lee W, Tonelli M, Cornilescu G, Stolarska M, Nierzwicki L, Czub J, Markley JL, Marszalek J, Ciesielski SJ, Craig EA PLoS One. 2019 May 15;14(5):e0217098. doi: 10.1371/journal.pone.0217098., eCollection 2019. PMID:31091298^[4]

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

References

↑ Otto H, Conz C, Maier P, Wolfle T, Suzuki CK, Jeno P, Rucknagel P, Stahl J, Rospert S. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10064-9. Epub 2005 Jul 7. PMID:16002468 doi:http://dx.doi.org/10.1073/pnas.0504400102
↑ Hundley HA, Walter W, Bairstow S, Craig EA. Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science. 2005 May 13;308(5724):1032-4. Epub 2005 Mar 31. PMID:15802566 doi:http://dx.doi.org/10.1126/science.1109247
↑ Richly H, Rocha-Viegas L, Ribeiro JD, Demajo S, Gundem G, Lopez-Bigas N, Nakagawa T, Rospert S, Ito T, Di Croce L. Transcriptional activation of polycomb-repressed genes by ZRF1. Nature. 2010 Dec 23;468(7327):1124-8. doi: 10.1038/nature09574. PMID:21179169 doi:http://dx.doi.org/10.1038/nature09574
↑ Shrestha OK, Sharma R, Tomiczek B, Lee W, Tonelli M, Cornilescu G, Stolarska M, Nierzwicki L, Czub J, Markley JL, Marszalek J, Ciesielski SJ, Craig EA. Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70. PLoS One. 2019 May 15;14(5):e0217098. doi: 10.1371/journal.pone.0217098., eCollection 2019. PMID:31091298 doi:http://dx.doi.org/10.1371/journal.pone.0217098

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6cgh"

@@ Line 1: / Line 1: @@
 ==Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)==
-<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6cgh' size='340' side='right'caption='[[6cgh]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6cgh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGH FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJC2, MPHOSPH11, MPP11, ZRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [https://pdbe.org/6cgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [https://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh 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=6cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgh OCA], [http://pdbe.org/6cgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgh RCSB], [http://www.ebi.ac.uk/pdbsum/6cgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DNJC2_HUMAN DNJC2_HUMAN]] Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.<ref>PMID:16002468</ref> <ref>PMID:15802566</ref> <ref>PMID:21179169</ref>
+[https://www.uniprot.org/uniprot/DNJC2_HUMAN DNJC2_HUMAN] Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'.<ref>PMID:16002468</ref> <ref>PMID:15802566</ref> <ref>PMID:21179169</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
 *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ciesielski, S J]]
+[[Category: Ciesielski SJ]]
-[[Category: Cornilescu, G]]
+[[Category: Cornilescu G]]
-[[Category: Craig, E A]]
+[[Category: Craig EA]]
-[[Category: Lee, W]]
+[[Category: Lee W]]
-[[Category: Markley, J L]]
+[[Category: Markley JL]]
-[[Category: Shrestha, O K]]
+[[Category: Shrestha OK]]
-[[Category: Tonelli, M]]
+[[Category: Tonelli M]]
-[[Category: Chaperone]]
-[[Category: Dnajc2]]
-[[Category: Hsp40]]
-[[Category: Hsp70]]
-[[Category: J-protein]]
-[[Category: Molecular chaperone]]
-[[Category: Mpp11]]
-[[Category: Zuotin]]

6cgh

From Proteopedia

Current revision

Solution structure of the four-helix bundle region of human J-protein Zuotin, a component of ribosome-associated complex (RAC)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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