Functional characterization of archaeal homologs of human nuclear RNase P proteins Rpp21 and Rpp29 provides insights into the molecular basis of their cooperativity in catalysis

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• 作者：Dan Jiangp>ap>p> ; p>p>1p> ; Kenta Izumip>bp>p> ; p>p>1p> ; Toshifumi Uedap>bp>p> ; p>p>2p> ; Kosuke Oshimap>bp> ; Takashi Nakashimap>ap>p> ; p>p>bp> ; Makoto Kimurap>ap>p> ; p>p>bp>p> ; p>p>mkimura@agr.kyushu-u.ac.jpp>
• 关键词：Archaeal homologs of human proteins Rpp21 and Rpp29 ; Pull-down assay ; Pyrococcus horikoshii ; Ribonuclease P proteins ; RNA-Binding protein
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：1 January 2017
• 年：2017
• 卷：482
• 期：1
• 页码：68-74
• 全文大小：1444 K
• 卷排序：482

文摘

RNase P proteins PhoRpp21 and PhoRpp29 synergistically function in RNase P catalysis. PhoRpp21 functions as an RNA-binding element in the PhoRpp21-PhoRpp29 complex. PhoRpp21 serves as a scaffold for PhoRpp29 in RNase P. PhoRpp21 binds the loop between P11 and P12 helices in the PhopRNA S-domain. The molecular basis for the cooperativity of PhoRpp21 and PhoRpp29 is presented.