减数分裂过程中中心粒蛋白 Fta2 磷酸化的影响

Q3 Medicine
遗传 Pub Date : 2024-07-01 DOI:10.16288/j.yczz.24-038
Zi-Han Ni, Yu Min, Ling-Ling Ma, Yoshinori Watanabe
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引用次数: 0

摘要

在减数分裂过程中,中心粒区域内的凝聚素定位缺陷会导致各种疾病。凝聚素的准确定位取决于 Mis4-Ssl3 加载复合体。虽然已知凝聚素在装载复合体的帮助下完成装载过程,但其在中心粒区域定位的机制仍不清楚。以前的研究表明,凝聚素在中心粒的定位是由中心粒蛋白的磷酸化介导的。在这项研究中,我们重点研究了 Fta2 蛋白,它是 Sim4 中心粒蛋白复合物的一个组成部分。通过生物信息学方法,我们确定了潜在的磷酸化位点,并在小鼠中构建了 fta2-9A 和 fta2-9D 突变体。通过检测噻苯咪唑(TBZ)的敏感性和荧光显微镜定位,对这些突变体的表型进行了鉴定。结果表明,Fta2磷酸化不会影响有丝分裂,但会影响减数分裂过程中的染色体分离。这项研究表明,Fta2 磷酸化对减数分裂至关重要,可能与减数分裂过程中凝聚素的特异性定位有关。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The effect of centromere protein Fta2 phosphorylation during meiosis.

During meiosis, defects in cohesin localization within the centromere region can result in various diseases. Accurate cohesin localization depends on the Mis4-Ssl3 loading complex. Although it is known that cohesin completes the loading process with the help of the loading complex, the mechanisms underlying its localization in the centromere region remain unclear. Previous studies suggest cohesin localization in the centromere is mediated by phosphorylation of centromeric proteins. In this study, we focused on the Fta2 protein, a component of the Sim4 centromere protein complex. Using bioinformatics methods, potential phosphorylation sites were identified, and fta2-9A and fta2-9D mutants were constructed in Schizosaccharomyces pombe. The phenotypes of these mutants were characterized through testing thiabendazole (TBZ) sensitivity and fluorescent microscopy localization. Results indicated that Fta2 phosphorylation did not impact mitosis but affected chromosome segregation during meiosis. This study suggests that Fta2 phosphorylation is vital for meiosis and may be related to the specific localization of cohesin during this process.

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遗传
遗传 Medicine-Medicine (all)
CiteScore
2.50
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0.00%
发文量
6699
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