This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4jpo

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:22, 4 August 2016

5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1

Structural highlights

4jpo is a 4 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	HSM3, YBR272C, YBR1740 (Baker's yeast), RPT1, CIM5, YTA3, YKL145W (Baker's yeast)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HSM3_YEAST] Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] [PRS7_YEAST] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).

Publication Abstract from PubMed

The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric alpha-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the alpha-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound alpha-pockets with poor specificity, except for Rpt6, which uniquely bound the alpha2/alpha3-pocket. Although the Rpt6 tail is not visualized within an alpha-pocket in mature proteasomes, it inserts into the alpha2/alpha3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme.

Reconfiguration of the proteasome during chaperone-mediated assembly.,Park S, Li X, Kim HM, Singh CR, Tian G, Hoyt MA, Lovell S, Battaile KP, Zolkiewski M, Coffino P, Roelofs J, Cheng Y, Finley D Nature. 2013 May 23;497(7450):512-6. doi: 10.1038/nature12123. Epub 2013 May 5. PMID:23644457^[8]

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

References

↑ Fedorova IV, Gracheva LM, Kovaltzova SV, Evstuhina TA, Alekseev SY, Korolev VG. The yeast HSM3 gene acts in one of the mismatch repair pathways. Genetics. 1998 Mar;148(3):963-73. PMID:9539417
↑ Merker JD, Datta A, Kolodner RD, Petes TD. The yeast HSM3 gene is not involved in DNA mismatch repair in rapidly dividing cells. Genetics. 2000 Jan;154(1):491-3. PMID:10681182
↑ Fedorova IV, Kovaltzova SV, Korolev VG. The yeast HSM3 gene is involved in DNA mismatch repair in slowly dividing cells. Genetics. 2000 Jan;154(1):495-6. PMID:10681183
↑ Fedorova IV, Kovaltzova SV, Gracheva LM, Evstuhina TA, Korolev VG. Requirement of HSM3 gene for spontaneous mutagenesis in Saccharomyces cerevisiae. Mutat Res. 2004 Oct 4;554(1-2):67-75. PMID:15450405 doi:10.1016/j.mrfmmm.2004.03.003
↑ Funakoshi M, Tomko RJ Jr, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 2009 May 29;137(5):887-99. Epub 2009 May 14. PMID:19446322 doi:S0092-8674(09)00526-1
↑ Le Tallec B, Barrault MB, Guerois R, Carre T, Peyroche A. Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell. 2009 Feb 13;33(3):389-99. doi: 10.1016/j.molcel.2009.01.010. PMID:19217412 doi:10.1016/j.molcel.2009.01.010
↑ Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, Finley D. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature. 2009 Jun 11;459(7248):861-5. PMID:19412159 doi:nature08063
↑ Park S, Li X, Kim HM, Singh CR, Tian G, Hoyt MA, Lovell S, Battaile KP, Zolkiewski M, Coffino P, Roelofs J, Cheng Y, Finley D. Reconfiguration of the proteasome during chaperone-mediated assembly. Nature. 2013 May 23;497(7450):512-6. doi: 10.1038/nature12123. Epub 2013 May 5. PMID:23644457 doi:10.1038/nature12123

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4jpo"

@@ Line 1: / Line 1: @@
 ==5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1==
 <StructureSection load='4jpo' size='340' side='right' caption='[[4jpo]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4jpo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JPO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4jpo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JPO FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSM3, YBR272C, YBR1740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), RPT1, CIM5, YTA3, YKL145W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSM3, YBR272C, YBR1740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPT1, CIM5, YTA3, YKL145W ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jpo RCSB], [http://www.ebi.ac.uk/pdbsum/4jpo PDBsum]</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=4jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpo OCA], [http://pdbe.org/4jpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jpo RCSB], [http://www.ebi.ac.uk/pdbsum/4jpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpo ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4jpo" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae s288c]]
+[[Category: Baker's yeast]]
 [[Category: Battaile, K P]]
 [[Category: Lovell, S]]

4jpo

From Proteopedia

Revision as of 22:22, 4 August 2016

5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox