SUMOylation is required for normal development of linear elements and wild-type meiotic recombination in Schizosaccharomyces pombe

SUMOylation is required for normal development of linear elements and wild-type meiotic recombination in Schizosaccharomyces pombe
复制标题

DOI:
10.1007/s00412-009-0241-5
复制
发表时间:
2010-02-01
期刊:
影响因子:
1.6
通讯作者:
Loidl, Josef
Loidl, Josef
中科院分区:
生物学3区
文献类型:
--
作者:
Spirek, Mario;Estreicher, Anna;Loidl, Josef

文献摘要

被引文献

相似文献

在裂殖酵母粟酒裂殖酵母中,联会复合体(SC)在减数分裂前期不形成。然而,出现了类似于SC轴向元件的结构,即所谓的线性元件(LinEs)。原位免疫组化显示Pmt 3(S. pombe's SUMO蛋白),表明LinEs的某些组分的SUMO化发生在减数分裂期间。SUMO连接酶Pli1的突变导致异常的LinE形成和减少的遗传重组,表明LinE的SUMO化在减数分裂重组的调节中起作用。TAP标记的Rec10蛋白质印迹分析表明,有一个Pli1依赖的翻译后修饰的这种蛋白质,这是一个主要的LinE组件和SC蛋白Red1的远亲同源物。质谱分析表明Rec10是磷酸化和泛素化的,但没有发现Rec10的SUMO化,这些发现表明LinE和Rec10的功能调节是通过Pli1依赖的SUMO化直接或间接调节Rec10的修饰。另一方面,MS分析证实了Rec10与已知的LinE组分Rec25、Rec27和Hop1的相互作用,并鉴定了减数分裂上调的蛋白质Mug20作为一种新的推定的LinE相关蛋白。
In the fission yeast, Schizosaccharomyces pombe, synaptonemal complexes (SCs) are not formed during meiotic prophase. However, structures resembling the axial elements of SCs, the so-called linear elements (LinEs) appear. By in situ immunostaining, we found Pmt3 (S. pombe's SUMO protein) transiently along LinEs, suggesting that SUMOylation of some component(s) of LinEs occurs during meiosis. Mutation of the SUMO ligase Pli1 caused aberrant LinE formation and reduced genetic recombination indicating a role for SUMOylation of LinEs for the regulation of meiotic recombination. Western blot analysis of TAP-tagged Rec10 demonstrated that there is a Pli1-dependent posttranslational modification of this protein, which is a major LinE component and a distant homolog of the SC protein Red1. Mass spectrometry (MS) analysis revealed that Rec10 is both phosphorylated and ubiquitylated, but no evidence for SUMOylation of Rec10 was found. These findings indicate that the regulation of LinE and Rec10 function is modulated by Pli1-dependent SUMOylation of LinE protein(s) which directly or indirectly regulates Rec10 modification. On the side, MS analysis confirmed the interaction of Rec10 with the known LinE components Rec25, Rec27, and Hop1 and identified the meiotically upregulated protein Mug20 as a novel putative LinE-associated protein.