Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes
| Autor: | Oerum, S, Roovers, M, Rambo, R, Kopec, J, Bailey, H, Fitzpatrick, F, Newman, J, Newman, W, Amberger, A, Zschocke, J, Droogmans, L, Oppermann, U, Yue, W |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular HSD10 RNA Mitochondrial Biochimie 3-Hydroxyacyl CoA Dehydrogenases Biologie moléculaire ribonuclease P (RNase P) HSD17B10 Methyltransferases Crystallography X-Ray Ribonuclease P transfer RNA (tRNA) RNA Transfer Multienzyme Complexes Protein Structure and Folding Scattering Small Angle RNA methylation RNA methyltransferase MRPP TRMT10C Humans PRORP Biologie cellulaire complex |
| Zdroj: | The Journal of biological chemistry, 293 (33 The Journal of Biological Chemistry Oerum, S, Roovers, M, Rambo, R P, Kopec, J, Bailey, H J, Fitzpatrick, F, Newman, J A, Newman, W G, Amberger, A, Zschocke, J, Droogmans, L, Oppermann, U & Yue, W W 2018, ' Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes ', Journal of Biological Chemistry, vol. 293, no. 33, pp. 12862-12876 . https://doi.org/10.1074/jbc.RA117.001286 |
| DOI: | 10.1074/jbc.ra117.001286 |
| Popis: | Mitochondrial tRNAs are transcribed as long polycistronic transcripts of precursor tRNAs and undergo posttranscriptional modifications such as endonucleolytic processing and methylation required for their correct structure and function. Among them, 5-end processing and purine 9 N1-methylation of mitochondrial tRNA are catalyzed by two proteinaceous complexes with overlapping subunit composition. The Mg2-dependent RNase P complex for 5-end cleavage comprises the methyltransferase domain– containing protein tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C/MRPP1), short-chain oxidoreductase hydroxysteroid 17-dehydroge-nase 10 (HSD17B10/MRPP2), and metallonuclease KIAA0391/ MRPP3. An MRPP1–MRPP2 subcomplex also catalyzes the formation of 1-methyladenosine/1-methylguanosine at position 9 using S-adenosyl-L-methionine as methyl donor. However, a lack of structural information has precluded insights into how these complexes methylate and process mitochondrial tRNA. Here, we used a combination of X-ray crystallography, interaction and activity assays, and small angle X-ray scattering (SAXS) to gain structural insight into the two tRNA modification complexes and their components. The MRPP1 N terminus is involved in tRNA binding and monomer–monomer self-interaction, whereas the C-terminal SPOUT fold contains key residues for S-adenosyl-L-methionine binding and N1-methylation. SCOPUS: ar.j info:eu-repo/semantics/published |
| Databáze: | OpenAIRE |
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