Journal Article

PUBDB-2024-01042

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure of the nuclease subunit of human mitochondrial RNase P

Reinhard, L.Extern* ; Sridhara, S.Extern*EMBL* ; Hallberg, B. M. (Corresponding author)

2015
Oxford Univ. Press Oxford

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Please use a persistent id in citations: doi:10.1093/nar/gkv481  doi:10.3204/PUBDB-2024-01042

Abstract: Mitochondrial 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.

Note: ISSN 1362-4962 not unique: **2 hits**.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

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