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Review
. 2017 Sep 3;8(5):461-468.
doi: 10.1080/19491034.2017.1330237. Epub 2017 Jun 19.

H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis

Affiliations
Review

H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis

Liying Wang et al. Nucleus. .

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.

Keywords: H2B ubiquitination; RNF20; evolution; meiosis; phylogenetic analysis.

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Figures

Figure 1.
Figure 1.
Multiple species phylogenetic tree of RNF20. Phylogenetic tree of RNF20 proteins was constructed by MEGA 6.0 with the Neighbor-Joining (NJ) method. We performed 1000 bootstrap replicates. And I, II, III represent different groups, with I representing animals, II representing plants, III representing fungi.
Figure 2.
Figure 2.
Multiple species phylogenetic tree of Rad6. The same method to that of RNF20 was used to construct this tree.
Figure 3.
Figure 3.
Multiple species phylogenetic tree of WAC and Lge1. The procedure to constuct the phylogenetic tree were the same to that of RNF20.
Figure 4.
Figure 4.
Phylogenetic tree and domain architectures of RNF20. Phylogenetic tree was shown at the left and the domain architectures were shown at right. The domain patterns were explained in the inset.

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