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首页> 外文期刊>Biochemistry >Domain Architecture of the DRpp29 Protein and Its Interaction with the RNA Subunit of Dictyostelium discoideum RNase P
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Domain Architecture of the DRpp29 Protein and Its Interaction with the RNA Subunit of Dictyostelium discoideum RNase P

机译：DRpp29蛋白的域结构及其与盘基网柄菌RNase P的RNA亚基的相互作用

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摘要

Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similaritiesnwith its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retainsndistinctive characteristics. In the present study, we report the molecular cloning and interaction details ofnDRpp29 and RNase P RNA, two subunits of the RNase P holoenzyme from D. discoideum. Electrophoreticnmobility shift assays exhibited that DRpp29 binds specifically to the RNase P RNA subunit, a feature that wasnfurther confirmed by themolecularmodeling of theDRpp29 structure.Moreover, deletionmutants ofDRpp29nwere constructed in order to investigate the domains ofDRpp29 that contribute to and/or are responsible for thendirect interaction with the D. discoideum RNase P RNA. A eukaryotic specific, lysine- and arginine-rich regionnwas revealed, which seems to facilitate the interaction between these two subunits. Furthermore, we tested thenability of wild-type and mutant DRpp29 to form active RNase P enzymatic particles with the Escherichia colinRNase P RNA.
机译：盘基网柄菌核RNase P是一种核糖核蛋白复合物，与高级真核生物的对应物（如人类酶）显示出相似性，但同时保留了显着特征。在本研究中，我们报道了来自D. discoideum的RNase P全酶的两个亚基nDRpp29和RNase P RNA的分子克隆和相互作用细节。电泳迁移率测定法显示DRpp29与RNase P RNA亚基特异性结合，这一特征通过DRpp29结构的分子模型进一步证实。此外，构建了DRpp29的缺失突变体，以研究DRpp29的结构域，这些结构域和/或负责与之直接相互作用。 D. discoideum核糖核酸酶P RNA。揭示了一个富含赖氨酸和精氨酸的真核特异性区域，这似乎促进了这两个亚基之间的相互作用。此外，我们测试了野生型和突变DRpp29与大肠埃希氏菌colinRNase P RNA形成活性RNase P酶促颗粒的能力。

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  • 来源
    《Biochemistry》 |2010年第50期|p.10714-10727|共14页
  • 作者

    Vassiliki Stamatopoulou Chrisavgi Toumpeki Andreas Tzakos Anastassios Vourekas and Denis Drainas;

  • 作者单位

    ‡Department of Biochemistry, School of Medicine, University of Patras, 26500 Patras, Greece, and §Department of Chemistry,Section of Organic Chemistry and Biochemistry, University of Ioannina, 45110 Ioannina, Greece.) Present address:Department of Pathology and LaboratoryMedicine, Division of Neuropathology, University of PennsylvaniaSchool of Medicine, Philadelphia, PA 19104.;

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