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  Structural basis of RNA processing by human mitochondrial RNase P

Bhatta, A., Dienemann, C., Cramer, P., & Hillen, H. (2021). Structural basis of RNA processing by human mitochondrial RNase P. Nature Structural and Molecular Biology, 28(9), 713-723. doi:10.1038/s41594-021-00637-y.

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 Creators:
Bhatta, A.1, Author              
Dienemann, C.2, Author              
Cramer, P.2, Author              
Hillen, H.1, Author              
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1Research Group Structure and Function of Molecular Machines, MPI for Biophysical Chemistry, Max Planck Society, ou_3265856              
2Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: Catalytic RNA, Cryoelectron microscopy, Mitochondria, RNA metabolism
 Abstract: Human mitochondrial transcripts contain messenger and ribosomal RNAs flanked by transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to liberate all RNA species. In contrast to nuclear or bacterial RNase P, mtRNase P is not a ribozyme but comprises three protein subunits that carry out RNA cleavage and methylation by unknown mechanisms. Here, we present the cryo-EM structure of human mtRNase P bound to precursor tRNA, which reveals a unique mechanism of substrate recognition and processing. Subunits TRMT10C and SDR5C1 form a subcomplex that binds conserved mitochondrial tRNA elements, including the anticodon loop, and positions the tRNA for methylation. The endonuclease PRORP is recruited and activated through interactions with its PPR and nuclease domains to ensure precise pre-tRNA cleavage. The structure provides the molecular basis for the first step of RNA processing in human mitochondria.

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Language(s): eng - English
 Dates: 2021-09-062021-09
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41594-021-00637-y
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 28 (9) Sequence Number: - Start / End Page: 713 - 723 Identifier: -