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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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In Vitro Analysis of E3 Ubiquitin Ligase Function
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An E2 accessory domain increases affinity for the anaphase-promoting complex and ensures E2 competition.

Juliet R Girard1, Jeanette L Tenthorey2, David O Morgan3

  • 1From the Departments of Physiology and Biochemistry and Biophysics and Tetrad Graduate Program, University of California, San Francisco, California 94143.

The Journal of Biological Chemistry
|August 26, 2015
PubMed
Summary

The anaphase-promoting complex/cyclosome (APC/C) uses its Ubc1 E2 enzyme

Keywords:
E3 ubiquitin ligasecell cycleubiquitinubiquitin-conjugating enzyme (E2 enzyme)yeast

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Ubiquitination Pathways

Background:

  • The anaphase-promoting complex/cyclosome (APC/C) is a crucial E3 ubiquitin ligase.
  • It collaborates with E2 enzymes Ubc4 and Ubc1 for polyubiquitination.
  • The competitive binding of Ubc4 and Ubc1 to the APC/C is not fully understood.

Purpose of the Study:

  • To investigate the role of the Ubc1 ubiquitin-associated (UBA) domain in APC/C interaction.
  • To elucidate the mechanism by which Ubc1 affinity is balanced with Ubc4.
  • To understand the contribution of the UBA domain to polyubiquitin chain formation.

Main Methods:

  • Site-directed mutagenesis to delete the UBA domain of Ubc1.
  • Affinity measurements of Ubc1 and its UBA-deleted mutant for the APC/C.
  • In vivo assays to assess Ubc1 function and E2 competition.

Main Results:

  • The C-terminal UBA domain of Ubc1 significantly enhances its affinity for the APC/C.
  • Deletion of the UBA domain reduces Ubc1-APC/C affinity and polyubiquitin chain length.
  • The UBA domain binds to the APC/C core, not to ubiquitin substrates or Ubc1 itself, facilitating competition with Ubc4.

Conclusions:

  • The UBA domain of Ubc1 is essential for its high-affinity binding to the APC/C.
  • This domain plays a critical role in balancing Ubc1 and Ubc4 competition.
  • Ubc1's UBA domain ensures efficient substrate polyubiquitination by modulating E2 enzyme affinity.