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An optimized protocol for acquiring and processing cryo-EM data of human 26S proteasome with M1-Ub6

  1. Author:
    Chen,Xiang
    Shi,Dan
    Zhang,Ping
    Walters,Kylie

  2. Author Address

    Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA., Kinase Complexes Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.,
    1. Year: 2021
    2. Date: Mar 19
    3. Epub Date: 2021 01 18
  2. Journal: STAR protocols
    1. 2
    2. 1
    3. Pages: 100278
  4. Type of Article: Article
  5. Article Number: 100278
  1. Abstract:

    The 26S proteasome is specialized for regulated protein degradation. It is formed by a regulatory particle (RP) that recognizes ubiquitinated substrates and caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Structural heterogeneity caused by dynamics makes it challenging to observe ubiquitin chains at the RP by cryogenic electron microscopy (cryo-EM). Here, we present a cryo-EM-based protocol we applied to study the human 26S proteasome with ubiquitin chains by using non-cleavable M1-linked hexaubiquitin (M1-Ub6) unanchored to a substrate. For complete details on the use and execution of this protocol, please refer to Chen et al. (2020).

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External Sources

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  2. DOI: 10.1016/j.xpro.2020.100278
  3. PMID: 33521680
  4. PMCID: PMC7820132
  5. PII : S2666-1667(20)30265-3

Library Notes

  1. Fiscal Year: FY2020-2021
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