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000604244 1001_ $$0P:(DE-H253)PIP1017112$$aReinhard, L.$$b0
000604244 245__ $$aStructure of the nuclease subunit of human mitochondrial RNase P
000604244 260__ $$aOxford$$bOxford Univ. Press$$c2015
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000604244 520__ $$aMitochondrial RNA polymerase produces long polycistronic precursors that contain the mRNAs, rRNAs and tRNAs needed for mitochondrial translation. Mitochondrial RNase P (mt-RNase P) initiates the maturation of the precursors by cleaving at the 5′ ends of the tRNAs. Human mt-RNase P is only active as a tripartite complex (mitochondrial RNase P proteins 1–3; MRPP1-3), whereas plant and trypanosomal RNase Ps (PRORPs)—albeit homologous to MRPP3—are active as single proteins. The reason for this discrepancy has so far remained obscure. Here, we present the crystal structure of human MRPP3, which features a remarkably distorted and hence non-productive active site that we propose will switch to a fully productive state only upon association with MRPP1, MRPP2 and pre-tRNA substrate. We suggest a mechanism in which MRPP1 and MRPP2 both deliver the pre-tRNA substrate and activate MRPP3 through an induced-fit process. 
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000604244 7001_ $$0P:(DE-H253)PIP1020963$$aSridhara, S.$$b1
000604244 7001_ $$0P:(DE-HGF)0$$aHallberg, B. M$$b2$$eCorresponding author
000604244 773__ $$0PERI:(DE-600)2205588-5$$a10.1093/nar/gkv481$$gVol. 43, no. 11, p. 5664 - 5672$$n11$$p5664 - 5672$$tNucleic acids symposium series$$v43$$x0305-1048$$y2015
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