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Updated: Feb 28, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis
Liying Wang1,2, Chunwei Cao1,2, Fang Wang1,2
1a State Key Laboratory of Stem Cell and Reproductive Biology , Institute of Zoology, Chinese Academy of Sciences , Beijing , P.R. China.
Abstract:
RNF20/Bre1 mediated H2B ubiquitination (H2Bub) has various physiologic functions. Recently, we found that H2Bub participates in meiotic recombination by promoting chromatin relaxation during meiosis. We then analyzed the phylogenetic relationships among the E3 ligase for H2Bub, its E2 Rad6 and their partner WW domain-containing adaptor with a coiled-coil (WAC) or Lge1, and found that the molecular mechanism underlying H2Bub is evolutionarily conserved from yeast to mammals. However, RNF20 has diverse physiologic functions in different organisms, which might be caused by the evolutionary divergency of their domain/motif architectures. In the current extra view, we not only elucidate the evolutionarily conserved molecular mechanism underlying H2Bub, but also discuss the diverse physiologic functions of RNF20 during meiosis.
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