Protein-protein interactions in the subunits of ribonuclease p in the hyperthermophilic archaeon Pyrococcus horikoshii OT3
Protein-protein interactions in the subunits of ribonuclease p in the hyperthermophilic archaeon Pyrococcus horikoshii OT3
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DOI：
10.1271/bbb.69.1209
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发表时间：
2005-06-01
影响因子：
1.6
通讯作者：
Kimura, M
中科院分区：
文献类型：
--
作者：
Kifusa, M;Fukuhara, H;Kimura, M
核糖核酸酶P （RNase P）是一种核糖核蛋白复合物，参与前体tRNA （pre-tRNA）的5'先导序列的加工。嗜热古细菌horikoshii焦球菌OT3的RNase P由RNA和5个蛋白亚基（Ph1481p、Ph1496p、Ph1601p、Ph1771p和Ph1877p）组成。利用酵母双杂交系统研究了A horikoshii OT3中5个RNase P蛋白亚基在体内的相互作用。分析表明，蛋白Ph1481p和Ph1601p分别与Ph1877p和Ph1771p相互作用较强，而Ph1481p与Ph1601p相互作用较弱。相比之下，Ph1496p与其他4个蛋白之间未检测到相互作用。共免疫沉淀分析证实。酵母双杂交试验获得的相互作用。
Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5' leader sequence of precursor tRNA (pre-tRNA). RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of RNA and five protein subunits (Ph1481p, Ph1496p, Ph1601p, Ph1771p, and Ph1877p). In vivo interactions among five protein subunits of RNase P in A horikoshii OT3 were examined using a yeast two-hybrid system. The analysis indicates that proteins Ph1481p and Ph1601p interact strongly with Ph1877p and Ph1771p respectively, whereas Ph1481p interacts moderately with Ph1601p. In contrast, no interaction was detected between Ph1496p and the other four proteins. Co-immunoprecipitation analysis confirmed the. interactions obtained by yeast two-hybrid assay.