The effect of centromere protein Fta2 phosphorylation during meiosis.

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
{"title":"The effect of centromere protein Fta2 phosphorylation during meiosis.","authors":"Zi-Han Ni, Yu Min, Ling-Ling Ma, Yoshinori Watanabe","doi":"10.16288/j.yczz.24-038","DOIUrl":null,"url":null,"abstract":"<p><p>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 <i>fta2-9A</i> and <i>fta2-9D</i> mutants were constructed in <i>Schizosaccharomyces pombe</i>. 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.</p>","PeriodicalId":35536,"journal":{"name":"遗传","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"遗传","FirstCategoryId":"1091","ListUrlMain":"https://doi.org/10.16288/j.yczz.24-038","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Medicine","Score":null,"Total":0}
引用次数: 0

Abstract

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.

减数分裂过程中中心粒蛋白 Fta2 磷酸化的影响
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。
求助全文
约1分钟内获得全文 求助全文
来源期刊
遗传
遗传 Medicine-Medicine (all)
CiteScore
2.50
自引率
0.00%
发文量
6699
期刊介绍:
文献相关原料
公司名称 产品信息 采购帮参考价格
上海源叶 噻苯咪唑(TBZ)
¥20.00~¥11800.00
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信