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==Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1==
==Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1==
<StructureSection load='7c7a' size='340' side='right'caption='[[7c7a]]' scene=''>
<StructureSection load='7c7a' size='340' side='right'caption='[[7c7a]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C7A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C7A FirstGlance]. <br>
<table><tr><td colspan='2'>[[7c7a]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_(strain_atcc_204508_/_s288c) Saccharomyces cerevisiae (strain atcc 204508 / s288c)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C7A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C7A FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7a OCA], [http://pdbe.org/7c7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c7a RCSB], [http://www.ebi.ac.uk/pdbsum/7c7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7a ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[7c79|7c79]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7a OCA], [http://pdbe.org/7c7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c7a RCSB], [http://www.ebi.ac.uk/pdbsum/7c7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/POP6_YEAST POP6_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/RMP1_YEAST RMP1_YEAST]] Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.<ref>PMID:15637077</ref>  [[http://www.uniprot.org/uniprot/POP3_YEAST POP3_YEAST]] Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.<ref>PMID:9029160</ref> <ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/POP7_YEAST POP7_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9618478</ref> <ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/RPP1_YEAST RPP1_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9308968</ref> <ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/POP1_YEAST POP1_YEAST]] Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.<ref>PMID:7926742</ref> <ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/POP8_YEAST POP8_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/POP4_YEAST POP4_YEAST]] Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P.<ref>PMID:9085845</ref> <ref>PMID:9620854</ref>  [[http://www.uniprot.org/uniprot/RMRP_YEAST RMRP_YEAST]] Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.<ref>PMID:7958920</ref>  [[http://www.uniprot.org/uniprot/POP5_YEAST POP5_YEAST]] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.<ref>PMID:9620854</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in pre-ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves tRNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-EM structures of Saccharomyces cerevisiae RNase MRP alone and in complex with a fragment of pre-rRNA. These structures combined with biochemical studies reveal that co-evolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely-defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts.
Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.,Lan P, Zhou B, Tan M, Li S, Cao M, Wu J, Lei M Science. 2020 Jun 25. pii: science.abc0149. doi: 10.1126/science.abc0149. PMID:32586950<ref>PMID:32586950</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7c7a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Baker's yeast]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lan P]]
[[Category: Ribonuclease P]]
[[Category: Lei M]]
[[Category: Lan, P]]
[[Category: Wu J]]
[[Category: Lei, M]]
[[Category: Wu, J]]
[[Category: Ribonuclease mrp]]
[[Category: Rna binding protein]]
[[Category: Rna-protein complex]]

Revision as of 14:41, 26 August 2020

Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1

Structural highlights

7c7a is a 13 chain structure with sequence from Baker's yeast and Saccharomyces cerevisiae (strain atcc 204508 / s288c). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Ribonuclease P, with EC number 3.1.26.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POP6_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[1] [RMP1_YEAST] Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.[2] [POP3_YEAST] Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.[3] [4] [POP7_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[5] [6] [RPP1_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[7] [8] [POP1_YEAST] Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.[9] [10] [POP8_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[11] [POP4_YEAST] Required for 5.8S rRNA and tRNA processing; associated with RNase MRP and RNase P.[12] [13] [RMRP_YEAST] Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.[14] [POP5_YEAST] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.[15]

Publication Abstract from PubMed

Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in pre-ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves tRNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-EM structures of Saccharomyces cerevisiae RNase MRP alone and in complex with a fragment of pre-rRNA. These structures combined with biochemical studies reveal that co-evolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely-defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts.

Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.,Lan P, Zhou B, Tan M, Li S, Cao M, Wu J, Lei M Science. 2020 Jun 25. pii: science.abc0149. doi: 10.1126/science.abc0149. PMID:32586950[16]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  2. ↑ Salinas K, Wierzbicki S, Zhou L, Schmitt ME. Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component. J Biol Chem. 2005 Mar 25;280(12):11352-60. Epub 2005 Jan 6. PMID:15637077 doi:http://dx.doi.org/M409568200
  3. ↑ Dichtl B, Tollervey D. Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo. EMBO J. 1997 Jan 15;16(2):417-29. PMID:9029160
  4. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  5. ↑ Stolc V, Katz A, Altman S. Rpp2, an essential protein subunit of nuclear RNase P, is required for processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6716-21. PMID:9618478
  6. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  7. ↑ Stolc V, Altman S. Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae. Genes Dev. 1997 Sep 15;11(18):2414-25. PMID:9308968
  8. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  9. ↑ Lygerou Z, Mitchell P, Petfalski E, Seraphin B, Tollervey D. The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. Genes Dev. 1994 Jun 15;8(12):1423-33. PMID:7926742
  10. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  11. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  12. ↑ Chu S, Zengel JM, Lindahl L. A novel protein shared by RNase MRP and RNase P. RNA. 1997 Apr;3(4):382-91. PMID:9085845
  13. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  14. ↑ Schmitt ME, Clayton DA. Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain. Genes Dev. 1994 Nov 1;8(21):2617-28. PMID:7958920
  15. ↑ Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. PMID:9620854
  16. ↑ Lan P, Zhou B, Tan M, Li S, Cao M, Wu J, Lei M. Structural insight into precursor ribosomal RNA processing by ribonuclease MRP. Science. 2020 Jun 25. pii: science.abc0149. doi: 10.1126/science.abc0149. PMID:32586950 doi:http://dx.doi.org/10.1126/science.abc0149

7c7a, resolution 2.80Å

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