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4owt

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Structural basis of SOSS1 complex assembly

Structural highlights

4owt is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

INT3_HUMAN Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.^[1] ^[2] Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites.^[3] ^[4]

Publication Abstract from PubMed

The SOSS1 complex comprising SOSSA, SOSSB1, and SOSSC senses single-stranded DNA (ssDNA) and promotes repair of DNA double-strand breaks (DSBs). But how SOSS1 is assembled and recognizes ssDNA remains elusive. The crystal structure of the N-terminal half of SOSSA (SOSSAN) in complex with SOSSB1 and SOSSC showed that SOSSAN serves as a scaffold to bind both SOSSB1 and SOSSC for assembly of the SOSS1 complex. The structures of SOSSAN/B1 in complex with a 12 nt ssDNA and SOSSAN/B1/C in complex with a 35 nt ssDNA showed that SOSSB1 interacts with both SOSSAN and ssDNA via two distinct surfaces. Recognition of ssDNA with a length of up to nine nucleotides is mediated solely by SOSSB1, whereas neither SOSSC nor SOSSAN are critical for ssDNA binding. These results reveal the structural basis of SOSS1 assembly and provide a framework for further study of the mechanism governing longer ssDNA recognition by the SOSS1 complex during DSB repair.

Structural Basis of SOSS1 Complex Assembly and Recognition of ssDNA.,Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H Cell Rep. 2014 Mar 27;6(6):982-91. doi: 10.1016/j.celrep.2014.02.020. Epub 2014, Mar 13. PMID:24630995^[5]

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

References

↑ Li Y, Bolderson E, Kumar R, Muniandy PA, Xue Y, Richard DJ, Seidman M, Pandita TK, Khanna KK, Wang W. HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response. J Biol Chem. 2009 Aug 28;284(35):23525-31. doi: 10.1074/jbc.C109.039586. Epub, 2009 Jul 14. PMID:19605351 doi:http://dx.doi.org/10.1074/jbc.C109.039586
↑ Huang J, Gong Z, Ghosal G, Chen J. SOSS complexes participate in the maintenance of genomic stability. Mol Cell. 2009 Aug 14;35(3):384-93. doi: 10.1016/j.molcel.2009.06.011. PMID:19683501 doi:http://dx.doi.org/10.1016/j.molcel.2009.06.011
↑ Li Y, Bolderson E, Kumar R, Muniandy PA, Xue Y, Richard DJ, Seidman M, Pandita TK, Khanna KK, Wang W. HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response. J Biol Chem. 2009 Aug 28;284(35):23525-31. doi: 10.1074/jbc.C109.039586. Epub, 2009 Jul 14. PMID:19605351 doi:http://dx.doi.org/10.1074/jbc.C109.039586
↑ Huang J, Gong Z, Ghosal G, Chen J. SOSS complexes participate in the maintenance of genomic stability. Mol Cell. 2009 Aug 14;35(3):384-93. doi: 10.1016/j.molcel.2009.06.011. PMID:19683501 doi:http://dx.doi.org/10.1016/j.molcel.2009.06.011
↑ Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. Structural Basis of SOSS1 Complex Assembly and Recognition of ssDNA. Cell Rep. 2014 Mar 27;6(6):982-91. doi: 10.1016/j.celrep.2014.02.020. Epub 2014, Mar 13. PMID:24630995 doi:http://dx.doi.org/10.1016/j.celrep.2014.02.020

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/4owt"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4owt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OWT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4owt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4owt OCA], [https://pdbe.org/4owt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4owt RCSB], [https://www.ebi.ac.uk/pdbsum/4owt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4owt ProSAT]</span></td></tr>
 </table>

4owt

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Current revision

Structural basis of SOSS1 complex assembly

Structural highlights

Function

Publication Abstract from PubMed

References

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