TY - JOUR
T1 - Structure of a proteasome Pba1-Pba2 complex implications for proteasome assembly, activation, and biological function
AU - Stadtmueller, Beth M.
AU - Kish-Trier, Erik
AU - Ferrell, Katherine
AU - Petersen, Charisse N.
AU - Robinson, Howard
AU - Myszka, David G.
AU - Eckert, Debra M.
AU - Formosa, Tim
AU - Hill, Christopher P.
PY - 2012/10/26
Y1 - 2012/10/26
N2 - Pba1-Pba2 facilitates proteasome α-ring assembly. Results: Pba1-Pba2 binds mature proteasomes using C-terminal motifs and sequesters α-subunitNtermini. It does not activate and is not degraded by isolated 20S proteasomes. Conclusion: Pba1-Pba2 is important for proteasome-dependent maintenance of mitochondrial function. The structure is consistent with multiple roles in proteasome assembly. Significance: Models of proteasome assembly and Pba1-Pba2 proteasome function are advanced.
AB - Pba1-Pba2 facilitates proteasome α-ring assembly. Results: Pba1-Pba2 binds mature proteasomes using C-terminal motifs and sequesters α-subunitNtermini. It does not activate and is not degraded by isolated 20S proteasomes. Conclusion: Pba1-Pba2 is important for proteasome-dependent maintenance of mitochondrial function. The structure is consistent with multiple roles in proteasome assembly. Significance: Models of proteasome assembly and Pba1-Pba2 proteasome function are advanced.
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U2 - 10.1074/jbc.M112.367003
DO - 10.1074/jbc.M112.367003
M3 - Article
C2 - 22930756
AN - SCOPUS:84868238774
SN - 0021-9258
VL - 287
SP - 37371
EP - 37382
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 44
ER -