Structure of a proteasome Pba1-Pba2 complex implications for proteasome assembly, activation, and biological function

Beth M. Stadtmueller, Erik Kish-Trier, Katherine Ferrell, Charisse N. Petersen, Howard Robinson, David G. Myszka, Debra M. Eckert, Tim Formosa, Christopher P. Hill

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)37371-37382
Number of pages12
JournalJournal of Biological Chemistry
Volume287
Issue number44
DOIs
StatePublished - Oct 26 2012
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Stadtmueller, B. M., Kish-Trier, E., Ferrell, K., Petersen, C. N., Robinson, H., Myszka, D. G., Eckert, D. M., Formosa, T., & Hill, C. P. (2012). Structure of a proteasome Pba1-Pba2 complex implications for proteasome assembly, activation, and biological function. Journal of Biological Chemistry, 287(44), 37371-37382. https://doi.org/10.1074/jbc.M112.367003