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7o6l

From Proteopedia

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Crystal structure of C. elegans ERH-2

Structural highlights

7o6l is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ERH2_CAEEL Required for chromosome segregation and cell division in early embryos (PubMed:31216475). Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Piwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. C. elegans piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5' and 3' processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We used biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: PID-1 governs 21U processing, whereas TOST-1 links PETISCO to an unknown process essential for early embryogenesis. Here, we show that PETISCO forms an octameric assembly with each subunit present in two copies. Determination of structures of the TOFU-6/PID-3 and PID-3/ERH-2 subcomplexes, supported by in vivo studies of subunit interaction mutants, allows us to propose a model for the formation of the TOFU-6/PID-3/ERH-2 core complex and its functionality in germ cells and early embryos. Using NMR spectroscopy, we demonstrate that TOST-1 and PID-1 bind to a common surface on ERH-2, located opposite its PID-3 binding site, explaining how PETISCO can mediate different cellular roles.

Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans.,Perez-Borrajero C, Podvalnaya N, Holleis K, Lichtenberger R, Karaulanov E, Simon B, Basquin J, Hennig J, Ketting RF, Falk S Genes Dev. 2021 Sep 1;35(17-18):1304-1323. doi: 10.1101/gad.348648.121. Epub 2021, Aug 19. PMID:34413138^[4]

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

References

↑ Cordeiro Rodrigues RJ, de Jesus Domingues AM, Hellmann S, Dietz S, de Albuquerque BFM, Renz C, Ulrich HD, Sarkies P, Butter F, Ketting RF. PETISCO is a novel protein complex required for 21U RNA biogenesis and embryonic viability. Genes Dev. 2019 Jul 1;33(13-14):857-870. doi: 10.1101/gad.322446.118. Epub 2019, May 30. PMID:31147388 doi:http://dx.doi.org/10.1101/gad.322446.118
↑ Zeng C, Weng C, Wang X, Yan YH, Li WJ, Xu D, Hong M, Liao S, Dong MQ, Feng X, Xu C, Guang S. Functional Proteomics Identifies a PICS Complex Required for piRNA Maturation and Chromosome Segregation. Cell Rep. 2019 Jun 18;27(12):3561-3572.e3. doi: 10.1016/j.celrep.2019.05.076. PMID:31216475 doi:http://dx.doi.org/10.1016/j.celrep.2019.05.076
↑ Zeng C, Weng C, Wang X, Yan YH, Li WJ, Xu D, Hong M, Liao S, Dong MQ, Feng X, Xu C, Guang S. Functional Proteomics Identifies a PICS Complex Required for piRNA Maturation and Chromosome Segregation. Cell Rep. 2019 Jun 18;27(12):3561-3572.e3. doi: 10.1016/j.celrep.2019.05.076. PMID:31216475 doi:http://dx.doi.org/10.1016/j.celrep.2019.05.076
↑ Perez-Borrajero C, Podvalnaya N, Holleis K, Lichtenberger R, Karaulanov E, Simon B, Basquin J, Hennig J, Ketting RF, Falk S. Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans. Genes Dev. 2021 Sep 1;35(17-18):1304-1323. doi: 10.1101/gad.348648.121. Epub 2021, Aug 19. PMID:34413138 doi:http://dx.doi.org/10.1101/gad.348648.121

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7o6l"

Categories: Caenorhabditis elegans | Large Structures | Falk S | Ketting RF

@@ Line 3: / Line 3: @@
 <StructureSection load='7o6l' size='340' side='right'caption='[[7o6l]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7o6l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7o6l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6L FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">erh-2, F35G12.11 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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]] 1.5&#8491;</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=7o6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6l OCA], [https://pdbe.org/7o6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6l RCSB], [https://www.ebi.ac.uk/pdbsum/7o6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ERH2_CAEEL ERH2_CAEEL]] Required for chromosome segregation and cell division in early embryos (PubMed:31216475). Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475).<ref>PMID:31147388</ref> <ref>PMID:31216475</ref> <ref>PMID:31216475</ref>
+[https://www.uniprot.org/uniprot/ERH2_CAEEL ERH2_CAEEL] Required for chromosome segregation and cell division in early embryos (PubMed:31216475). Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475).<ref>PMID:31147388</ref> <ref>PMID:31216475</ref> <ref>PMID:31216475</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Caeel]]
+[[Category: Caenorhabditis elegans]]
 [[Category: Large Structures]]
-[[Category: Falk, S]]
+[[Category: Falk S]]
-[[Category: Ketting, R F]]
+[[Category: Ketting RF]]
-[[Category: Enhancer of rudimentary erh homodimer]]
-[[Category: Protein binding]]

7o6l

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Current revision

Crystal structure of C. elegans ERH-2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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