4.8 Article

Molecular convergence by differential domain acquisition is a hallmark of chromosomal passenger complex evolution

出版社

NATL ACAD SCIENCES
DOI: 10.1073/pnas.2200108119

关键词

cell division; microtuble cytoskeleton; evolution

资金

  1. Nederlandse Organisatie voor Wetenschappelijk Onderzoek [VI.Veni.202.223]
  2. Deutsche Forschungsgemeinschaft [SCHN 736/8-1]
  3. Ohsumi Frontier Science Foundation
  4. Japan Society for the Promotion of Science [JP21K06215]

向作者/读者索取更多资源

A study identified BORI1 and BORI2 as Survivin-like proteins in plants, which are essential for proper development. These proteins bind to phosphorylated histone H3, facilitating the association of CPC with chromatin. The presence of a helical domain that promotes complex formation with other scaffold components is a shared feature of Survivin-type proteins in animals and plants, and the addition of a phosphate-binding domain evolved independently in different eukaryotic groups.
The chromosomal passenger complex (CPC) is a heterotetrameric regulator of eukaryotic cell division, consisting of an Aurora-type kinase and a scaffold built of INCENP, Borealin, and Survivin. While most CPC components are conserved across eukaryotes, orthologs of the chromatin reader Survivin have previously only been found in animals and fungi, raising the question of how its essential role is carried out in other eukaryotes. By characterizing proteins that bind to the Arabidopsis Borealin ortholog, we identified BOREALIN RELATED INTERACTOR 1 and 2 (BORI1 and BORI2) as redundant Survivin-like proteins in the context of the CPC in plants. Loss of BORI function is lethal and a reduced expression of BORIs causes severe developmental defects. Similar to Survivin, we find that the BORIs bind to phosphorylated histone H3, relevant for correct CPC association with chromatin. However, this interaction is not mediated by a BIR domain as in previously recognized Survivin orthologs but by an FHA domain, a widely conserved phosphate-binding module. We find that the unifying criterion of Survivin-type proteins is a helix that facilitates complex formation with the other two scaffold components and that the addition of a phosphate-binding domain, necessary for concentration at the inner centromere, evolved in parallel in different eukaryotic groups. Using sensitive similarity searches, we find conservation of this helical domain between animals and plants and identify the missing CPC component in most eukaryotic supergroups. Interestingly, we also detect Survivin orthologs without a defined phosphate-binding domain, likely reflecting the situation in the last eukaryotic common ancestor.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据