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依赖于核糖体的NTP酶YchF和YihA的结合特性及酶活性研究
Distinct Binding and Enzymatic Activities of Two Ribosome-dependent NTPases YchF and YihA
投稿时间:2016-04-08  修订日期:2016-05-16
中文关键词:  YchF,YihA/YsxC,ATP酶,GTP酶,核糖体组装,GTP酶激活蛋白,翻译调控
英文关键词:YchF, YihA/YsxC, ATPase, GTPase, Ribosome assembly, GTPase-activating protein, translation regulation
基金项目:国家自然科学基金资助项目 (31422016, 31470722)
作者单位E-mail
孔梦媛 清华大学生命科学学院北京 100084 kongmengyuan1112@163.com 
闫凯歌 清华大学生命科学学院北京 100084  
马成英 清华大学生命科学学院北京 100084  
高宁 清华大学生命科学学院北京 100084 ninggao@mail.tsinghua.edu.cn 
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中文摘要:
      P-环NTP酶(GTP 酶和ATP酶)普遍存在于真核生物和原核生物中,参与调节不同的细胞进程.YchF和YihA是细菌中两种高度保守的NTP酶,但其生理功能仍然不清楚.之前的研究表明这两种NTP酶可以与核糖体或者核糖体亚基结合.我们检测了在不同核苷酸存在的情况下,大肠杆菌YchF和YihA蛋白与核糖体30S、50S、70S颗粒的结合情况,同时也探究了核糖体亚基的结合是否与NTP酶活性的激活有关.数据表明YchF与70S结合,YihA与50S结合.70S核糖体能同时激活YchF的ATP酶和GTP酶活性.然而YihA的GTP酶活性可以分别被50S和70S激活,并且70S呈现了8.8倍的激活效应.这些数据为进一步研究这两种保守的NTPase的生理功能奠定了基础.
英文摘要:
      P-loop NTPases (GTPase and ATPase) are widely employed in both prokaryotes and eukaryotes to regulate various cellular processes. YchF and YihA are two highly conserved NTPases in bacteria, but their cellular roles remain elusive. Previous data revealed that the ribosome or ribosomal subunits are binding partners of these two NTPases. Here, we examined the binding preferences of Escherichia coli YchF and YihA to the 30S, 50S and 70S ribosomes in the presence of different nucleotides, and assayed whether these binding preferences were associated with the stimulation of their NTPase activities. Our data show that YchF and YihA display a strong preference for the 70S and 50S, respectively. While the 70S ribosome, but not the 50S or 30S, promotes both the ATPase and GTPase activities of YchF, YihA responds to both the 50S and 70S, with the moderate GTPase stimulation (~8.8 fold) seen in the presence of the 70S ribosome.
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