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| == Structural insights == | | == Structural insights == |
| The active site of RNase P contains metal ions. Specifically, in the RNP-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. | | The active site of RNase P contains metal ions. Specifically, in the RNP-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. |
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| | A topic page on the RNP-based ''S. cerevisiae'' RNase P is found [[yeast RNase P|here]] |
| </StructureSection> | | </StructureSection> |
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| A topic page on the RNP-based ''S. cerevisiae'' RNase P is found [[yeast RNase P|here]]
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| == 3D Structures of RNase P == | | == 3D Structures of RNase P == |
Revision as of 19:10, 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 (RNP) 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 RNP-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.
A topic page on the RNP-based S. cerevisiae RNase P is found here
- ↑ 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
here - RNP-based RNase P bound to pre-tRNA substrate- 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
1a6f
1d6t
1nz0
1oqk
1ts9
1tsf
1v76
1v77
1x0t
2av5
2czv
2k3r
2ki7
2ljp
2zae
3dhs
3iab
3q1q
3q1r
3wyz
3wz0
4g23
4g24
4g25
4g26
4jg4
4xgl
4xgm
5diz
5ft9
6agb
6ah3
6ahr
6ahu
6ahv
6bv5
6bv6
6bv8
6bv9
6cqc
6cwx
6d1r
6k0a
6k0b
6max
See Also
References
proteopedia link