The chromosome axis controls meiotic events through a hierarchical assembly of HORMA domain proteins.
The chromosome axis controls meiotic events through a hierarchical assembly of HORMA domain proteins.
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DOI：
10.1016/j.devcel.2014.09.013
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发表时间：
2014-11-24
影响因子：
11.8
通讯作者：
Corbett, Kevin D.
中科院分区：
文献类型：
--
作者：
Kim, Yumi;Rosenberg, Scott C.;Kugel, Christine L.;Kostow, Nora;Rog, Ofer;Davydov, Vitaliy;Su, Tiffany Y.;Dernburg, Abby F.;Corbett, Kevin D.
HORMA 结构域家族的蛋白质在减数分裂期间的染色体组织和动力学中发挥着核心但人们知之甚少的作用。在秀丽隐杆线虫中，四种这样的蛋白质（HIM-3、HTP-1、HTP-2 和 HTP-3）具有不同但重叠的功能。通过结合生化、结构和体内分析，我们发现这些蛋白质通过其 HORMA 结构域与其伴侣 C 末端尾部内的同源肽结合形成分层复合物，类似于 Mad2 的“安全带”结合机制。这些相互作用对于将 HIM-3、HTP-1 和 HTP-2 招募到染色体轴至关重要。 HTP-3 除了将其他 HORMA 结构域蛋白募集到轴外，还在姐妹染色单体凝聚和双链断裂形成中发挥独立作用。最后，我们发现哺乳动物 HORMAD1 结合在其自身 C 端和 HORMAD2 C 端发现的肽基序，表明这种分子间缔合模式是真核生物减数分裂染色体结构的保守特征。
Proteins of the HORMA domain family play central but poorly understood roles in chromosome organization and dynamics during meiosis. In C. elegans, four such proteins (HIM-3, HTP-1, HTP-2, and HTP-3) have distinct but overlapping functions. Through combined biochemical, structural, and in vivo analysis, we find that these proteins form hierarchical complexes through binding of their HORMA domains to cognate peptides within their partners’ C-terminal tails, analogous to the “safety belt” binding mechanism of Mad2. These interactions are critical for recruitment of HIM-3, HTP-1, and HTP-2 to chromosome axes. HTP-3, in addition to recruiting the other HORMA domain proteins to the axis, plays an independent role in sister chromatid cohesion and double-strand break formation. Finally, we find that mammalian HORMAD1 binds a peptide motif found both at its own C-terminus and that of HORMAD2, indicating that this mode of intermolecular association is a conserved feature of meiotic chromosome structure in eukaryotes.
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