RNase P: Difference between revisions

Latest revision as of 20:35, 2 September 2019

Function

RNase P is a ribonuclease that processes 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]^[3]

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.^[4] In yeast, the proteins of RNase P also bind telomerase.^[5]

Sydney Altman shared in the 1989 Nobel Prize for his work on the catalytic properties of the RNP-based RNase P, as described here.

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.

Articles in Proteopedia concerning RNase P include:

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
↑ Engelke DR, Fierke CA. The evolution of RNase P. RNA. 2015 Apr;21(4):517-8. doi: 10.1261/rna.050732.115. PMID:25780121 doi:https://dx.doi.org/10.1261/rna.050732.115
↑ 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

3D Structures of RNase P

Updated on 02-September-2019

Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.

RNP-based RNase P

ribonuclease - RNP-based RNase P - S. cerevisiae
transfer RNAs - RNP-based RNase P bound to pre-tRNA substrate - S. cerevisiae

Protein-only RNase P

here - nuclear PRORP2 - Arabidopsis thaliana
here -mitochondrial and chloroplast PRORP1 - Arabidopsis thaliana

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

References

Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur

[1] 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

[2] 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

[3] Engelke DR, Fierke CA. The evolution of RNase P. RNA. 2015 Apr;21(4):517-8. doi: 10.1261/rna.050732.115. PMID:25780121 doi:https://dx.doi.org/10.1261/rna.050732.115

[4] 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

[5] 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

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-<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='' pspeed='8>
+[[Image:6ah3_labeled_solid.png|left|400px]]
 == 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''' is a [[Ribonuclease|ribonuclease]] that processes 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 (RNP) complexes; however, a few protein-only RNase Ps have been described.<ref>PMID:23322041</ref><ref>PMID:25780121</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>
+Sydney Altman shared in the 1989 Nobel Prize for his work on the catalytic properties of the RNP-based RNase P, as described [[RNase P Nobel Prizes|here]].
 == 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.
+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.
+Articles in Proteopedia concerning '''RNase P''' include:
+*  A topic page on the RNP-based ''S. cerevisiae'' RNase P is found [[yeast RNase P|here]]
 </StructureSection>
 == 3D Structures of RNase P ==
@@ Line 15: / Line 24: @@
 Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.
-Structural insights into protein-only RNase P complexed with tRNA
-[[6ahv]] - RNP-based RNase P - ''S. cerevisiae'' <br />
+'''RNP-based RNase P'''
-[[6ah3]] - RNP-based RNase P bound to pre-tRNA - ''S. cerevisiae''  <br />
+[[6agb]] - RNP-based RNase P - ''S. cerevisiae'' <br />
+[[6ah3]] - RNP-based RNase P bound to pre-tRNA substrate - ''S. cerevisiae''  <br />
+'''Protein-only RNase P'''
+[[5diz]] - nuclear PRORP2 - ''Arabidopsis thaliana''  <br />
+[[4g23]] -mitochondrial and chloroplast PRORP1 - ''Arabidopsis thaliana''  <br />
@@ Line 50: / Line 65: @@
 bv8
 bv9
+a6f
+d6t
+nz0
+oqk
+ts9
+tsf
+v76
+v77
+x0t
+av5
+czv
+k3r
+ki7
+ljp
+zae
+dhs
+iab
+q1q
+q1r
+wyz
+wz0
+g23
+g24
+g25
+g26
+jg4
+xgl
+xgm
+diz
+ft9
+agb
+ah3
+ahr
+ahu
+ahv
+bv5
+bv6
+bv8
+bv9
+cqc
+cwx
+d1r
+k0a
+k0b
+max
 ==See Also==
+*[[Ribozyme]]
 *[[Transfer RNA (tRNA)]]
 *[[Ribosome|The Ribosome]]
+*[[Ribonuclease]]
 == References ==
@@ Line 62: / Line 131: @@
 [[Category:Topic Page]]
+[[Category:Rnase_p|RNase P]]
+[[Category:Ribonuclease_P|Ribonuclease_P]]

RNase P: Difference between revisions

Latest revision as of 20:35, 2 September 2019

Function

Structural insights

3D Structures of RNase P

See Also

References

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools