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-Structure paper
タイトル | Reconfiguration of the proteasome during chaperone-mediated assembly. |
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ジャーナル・号・ページ | Nature, Vol. 497, Issue 7450, Page 512-516, Year 2013 |
掲載日 | 2013年5月23日 |
![]() | Soyeon Park / Xueming Li / Ho Min Kim / Chingakham Ranjit Singh / Geng Tian / Martin A Hoyt / Scott Lovell / Kevin P Battaile / Michal Zolkiewski / Philip Coffino / Jeroen Roelofs / Yifan Cheng / Daniel Finley / ![]() |
PubMed 要旨 | The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting ...The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-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 α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes, it inserts into the α2/α3-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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 5 - 9.6 Å |
構造データ | ![]() EMDB-5593: ![]() EMDB-5611: ![]() EMDB-5612: ![]() EMDB-5613: ![]() EMDB-5614: ![]() EMDB-5615: ![]() EMDB-5616: ![]() EMDB-5617: ![]() PDB-4jpo: |
由来 |
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![]() | CHAPERONE/HYDROLASE / Hsm3 / Chaperone / Proteasome / Protein Complex / CHAPERONE-HYDROLASE complex |