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| <StructureSection load='6ah3' size='350' side='right' caption=Yeast RNase P bound to pre-tRNA (PDB entry [[6ah3]])' scene='46/468224/Cv/1'> | | <StructureSection load='6ah3' size='350' side='right' caption=Yeast RNase P bound to pre-tRNA (PDB entry [[6ah3]])' scene=''> |
| == Function == | | == Function == |
| '''RNase P'' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref>
| | ''RNase P'' processing the 5′ end of pre-[[Transfer RNA (tRNA)|transfer RNAs]] as well as other RNA molecules.<ref>PMID:28697848</ref>. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref> |
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| In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.<ref>PMID:19395864</ref> In yeast, the proteins of RNase P also bind telomerase.<ref>PMID:27156450</ref> | | In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.<ref>PMID:19395864</ref> In yeast, the proteins of RNase P also bind telomerase.<ref>PMID:27156450</ref> |
Revision as of 18:50, 2 September 2019
| Function
RNase P processing the 5′ end of pre-transfer RNAs as well as other RNA molecules.[1]. Most RNase Ps are complexes of proteins and RNAs, termed ribonucleoprotein complexes; however, a few protein-only RNase Ps have been described.[2]
In eukaryotes, the RNase P proteins have been found to have other roles. For example, many of the proteins are shared with a related RNase P, the small nucleolar RNase MRP, that is involved in processing ribosomal RNA.[3] In yeast, the proteins of RNase P also bind telomerase.[4]
Structural insights
The active site of RNase P contains metal ions. Specifically, in the RNA-based RNase P, the ions at the active site are magnesium, and they seem to be zinc-based metallonucleases in the case of Arabidopsis proteinaceous RNase P.
- ↑ Jarrous N. Roles of RNase P and Its Subunits. Trends Genet. 2017 Sep;33(9):594-603. doi: 10.1016/j.tig.2017.06.006. Epub 2017, Jul 8. PMID:28697848 doi:https://dx.doi.org/10.1016/j.tig.2017.06.006
- ↑ Gobert A, Pinker F, Fuchsbauer O, Gutmann B, Boutin R, Roblin P, Sauter C, Giege P. Structural insights into protein-only RNase P complexed with tRNA. Nat Commun. 2013;4:1353. doi: 10.1038/ncomms2358. PMID:23322041 doi:https://dx.doi.org/10.1038/ncomms2358
- ↑ Davila Lopez M, Rosenblad MA, Samuelsson T. Conserved and variable domains of RNase MRP RNA. RNA Biol. 2009 Jul;6(3):208-20. Epub 2009 Jul 30. PMID:19395864
- ↑ Lemieux B, Laterreur N, Perederina A, Noel JF, Dubois ML, Krasilnikov AS, Wellinger RJ. Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP. Cell. 2016 May 19;165(5):1171-1181. doi: 10.1016/j.cell.2016.04.018. Epub 2016, May 5. PMID:27156450 doi:https://dx.doi.org/10.1016/j.cell.2016.04.018
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3D Structures of RNase P
Updated on 02-September-2019
Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.
Structural insights into protein-only RNase P complexed with tRNA
transfer RNAs - RNP-based RNase P - S. cerevisiae
6ah3 - RNP-based RNase P bound to pre-tRNA - S. cerevisiae
1jox
1jp0
1u9s
2a2e
2k3r
2ki7
2vrt
3iab
3q1q
3q1r
4g23
4g24
4g25
4g26
4xgl
4xgm
5diz
5xtm
6ahv
6bv5
6bv6
6bv8
6bv9
See Also
References
