| 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
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