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Expression, purification, and properties of the Ubc4/5 family of E2 enzymes

  1. Author:
    Lorick, K. L.
    Jensen, J. P.
    Weissman, A. M.

  2. Author Address

    Lorick, KL, NCI, Lab Prot Dynam & Signaling, Canc Res Ctr, Frederick, MD 21702 USA; NCI, Lab Prot Dynam & Signaling, Canc Res Ctr, Frederick, MD 21702 USA.
    1. Year: 2005
  2. Book Title: Methods in Enzymology
  3. Series Title: Methods in enzymology
    1. 398
    2. Pages: 54-68
  5. Type of Work: Review
  1. Abstract:

    Ubiquitin-conjugating enzymes (E2s) play a central role in ubiquitylation. They function to bridge the first, nonspecific step of ubiquitin activation by El with the transfer of activated ubiquitin to substrates by substrate-specific E3s. While sharing a common core UBC domain, members of this family exhibit significant specificity in their physical and functional interactions with E3s. Among the families of E2s, members of the yeast Ubc4/5 family are particularly well conserved in higher metazoans. In humans, these are represented by the UbcH5 family. Members of this ubiqutiously expressed family show a capacity to interact with a wide range of E3s from both HECT and RING finger families, making them particularly useful tools in the laboratory. Using the UbcH5 family as a prototype, this chapter describes methods for the expression, purification, and characterization of E2 enzymes in vitro and some of the basics for their use in experiments in cells

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