AI Article Synopsis
- RNF20/Bre1 is responsible for H2B ubiquitination (H2Bub), which plays a crucial role in various physiological processes, including meiotic recombination by enhancing chromatin relaxation.
- The study examined the evolutionary relationships of the E3 ligase for H2Bub and its associated proteins and found that the mechanisms of H2Bub are conserved across species from yeast to mammals.
- Despite this conservation, RNF20 exhibits different physiological functions in various organisms, likely due to differences in their domain/motif structures resulting from evolutionary changes.
Article 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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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5703235 | PMC |
| http://dx.doi.org/10.1080/19491034.2017.1330237 | DOI Listing |
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