Protein-protein interactions with subunits of human nuclear RNase P.
Protein-protein interactions with subunits of human nuclear RNase P.
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DOI：
10.1073/pnas.98.3.920
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发表时间：
2001-01
影响因子：
11.1
通讯作者：
T. Jiang;Sidney Altman
中科院分区：
文献类型：
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作者：
T. Jiang;Sidney Altman
利用酵母双杂交系统分析了人核RNase P蛋白亚基之间的相互作用以及与HeLa细胞cDNA文库中编码的其他相互作用伙伴之间的相互作用。亚基hpop 1、Rpp 21、Rpp 29、Rpp 30、Rpp 38和Rpp 40参与全酶复合物中广泛但较弱的蛋白质-蛋白质相互作用。发现Rpp 14、Rpp 20和Rpp 30与cDNA文库中编码的蛋白质具有强相互作用。小的热休克蛋白27，在双杂交试验中与Rpp 20相互作用，在亲和层析过程中与Rpp 20结合，可以发现与高度纯化的RNase P相关，并增强其活性。在HeLa细胞核中的RNase P活性也在热休克应激下增加。
A yeast two-hybrid system was used to analyze interactions among the protein subunits of human nuclear RNase P themselves and with other interacting partners encoded in a HeLa cell cDNA library. Subunits hpop1, Rpp21, Rpp29, Rpp30, Rpp38, and Rpp40 are involved in extensive, but weak, protein-protein interactions in the holoenzyme complex. Rpp14, Rpp20, and Rpp30 were found to have strong interactions with proteins encoded in the cDNA library. The small heat shock protein 27, which interacts with Rpp20 in the two-hybrid assay, binds to Rpp20 during affinity chromatography and can be found to be associated with, and enhances the activity of, highly purified RNase P. RNase P activity in HeLa cell nuclei also increases under the stress of heat shock.