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| | <StructureSection load='6tzn' size='340' side='right'caption='[[6tzn]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='6tzn' size='340' side='right'caption='[[6tzn]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TZN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TZN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pof8, SPAC17G6.17 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tzn OCA], [https://pdbe.org/6tzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tzn RCSB], [https://www.ebi.ac.uk/pdbsum/6tzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tzn ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tzn OCA], [https://pdbe.org/6tzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tzn RCSB], [https://www.ebi.ac.uk/pdbsum/6tzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tzn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/POF8_SCHPO POF8_SCHPO]] RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:29422501, PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1 (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division (PubMed:29422501, PubMed:29422503, PubMed:29422664).<ref>PMID:29422501</ref> <ref>PMID:29422503</ref> <ref>PMID:29422664</ref>
| + | [https://www.uniprot.org/uniprot/POF8_SCHPO POF8_SCHPO] RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:29422501, PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1 (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division (PubMed:29422501, PubMed:29422503, PubMed:29422664).<ref>PMID:29422501</ref> <ref>PMID:29422503</ref> <ref>PMID:29422664</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | La-related proteins 7 (LARP7) are a class of RNA chaperones that bind the 3' ends of RNA and are constitutively associated with their specific target RNAs. In metazoa, Larp7 binds to the long non-coding 7SK RNA as a core component of the 7SK RNP, a major regulator of eukaryotic transcription. In the ciliate Tetrahymena the LARP7 protein p65 is a component of telomerase, an essential ribonucleoprotein complex that maintains the telomeric DNA at eukaryotic chromosome ends. p65 is important for the ordered assembly of telomerase RNA (TER) with telomerase reverse transcriptase. Unexpectedly, Schizosaccharomyces pombe Pof8 was recently identified as a LARP7 protein and a core component of fission yeast telomerase essential for biogenesis. LARP7 proteins have a conserved N-terminal La motif and RRM1 (La module) and C-terminal RRM2 with specific RNA substrate recognition attributed to RRM2, first structurally characterized in p65 as an atypical RRM named xRRM. Here we present the X-ray crystal structure and NMR studies of S. pombe Pof8 RRM2. Sequence and structure comparison of Pof8 RRM2 to p65 and human Larp7 xRRMs reveals conserved features for RNA binding with the main variability in the length of the non-canonical helix alpha3. This study shows that Pof8 has conserved xRRM features, providing insight into TER recognition and the defining characteristics of the xRRM.
| + | |
| - | | + | |
| - | Structure of S. pombe telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins.,Basu R, Eichhorn CD, Cheng R, Peterson RD, Feigon J RNA Biol. 2020 Nov 1:1-12. doi: 10.1080/15476286.2020.1836891. PMID:33131423<ref>PMID:33131423</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6tzn" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fission yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Basu, R S]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Cascio, D]] | + | [[Category: Basu RS]] |
| - | [[Category: Eichhorn, C D]] | + | [[Category: Cascio D]] |
| - | [[Category: Feigon, J]] | + | [[Category: Eichhorn CD]] |
| - | [[Category: Larp7]] | + | [[Category: Feigon J]] |
| - | [[Category: Lsm binding]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rrm]]
| + | |
| Structural highlights
Function
POF8_SCHPO RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:29422501, PubMed:29422503, PubMed:29422664). Specifically binds telomerase RNA ter1 and promotes assembly of ter1 with catalytic subunit trt1 (PubMed:29422501, PubMed:29422503). Telomerase is a ribonucleoprotein enzyme essential that copies new telomeric repeats onto chromosome ends and functions to maintain cell division (PubMed:29422501, PubMed:29422503, PubMed:29422664).[1] [2] [3]
References
- ↑ Collopy LC, Ware TL, Goncalves T, I Kongsstovu S, Yang Q, Amelina H, Pinder C, Alenazi A, Moiseeva V, Pearson SR, Armstrong CA, Tomita K. LARP7 family proteins have conserved function in telomerase assembly. Nat Commun. 2018 Feb 8;9(1):557. doi: 10.1038/s41467-017-02296-4. PMID:29422501 doi:http://dx.doi.org/10.1038/s41467-017-02296-4
- ↑ Mennie AK, Moser BA, Nakamura TM. LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast. Nat Commun. 2018 Feb 8;9(1):586. doi: 10.1038/s41467-018-02874-0. PMID:29422503 doi:http://dx.doi.org/10.1038/s41467-018-02874-0
- ↑ Paez-Moscoso DJ, Pan L, Sigauke RF, Schroeder MR, Tang W, Baumann P. Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast. Nat Commun. 2018 Feb 8;9(1):587. doi: 10.1038/s41467-017-02284-8. PMID:29422664 doi:http://dx.doi.org/10.1038/s41467-017-02284-8
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