Crystal structure of SFPQ-NONO heterodimer

The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous exi...

Full description

Saved in:
Bibliographic Details
Published in:Biochimie 2022-07, Vol.198, p.1-7
Main Authors: Schell, Bianca, Legrand, Pierre, Fribourg, Sébastien
Format: Article
Language:English
Subjects:
DBHS
Heterodimer
Paraspeckle
Structure
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933
cites cdi_FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933
container_end_page 7
container_issue
container_start_page 1
container_title Biochimie
container_volume 198
creator Schell, Bianca
Legrand, Pierre
Fribourg, Sébastien
description The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous existence of six different dimeric complexes that sustain their function in many cellular processes such as pre-mRNA splicing, innate immunity, transcriptional regulation. In order to perform a complete structural analysis of all possible DBHS dimers, we have solved the crystal structure of the missing DBHS heterodimer SFPQ-NONO at 3.0 Å resolution. We identify subtle changes in amino acid composition and local secondary structure of the NOPS region orientation that may modulate affinity between complexes. Interestingly this area is found mutated in aggressive skin cancers and adenocarcinomas. -Structure of SFPQ-NONO heterodimer-Systematic structural analysis of all DBHS dimers-Identification of potential sites involved in fine-tuning dimer affinity
doi_str_mv 10.1016/j.biochi.2022.02.011
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2636145946</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0300908422000517</els_id><sourcerecordid>2636145946</sourcerecordid><originalsourceid>FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933</originalsourceid><addsrcrecordid>eNp9kF9LwzAUxYMobk6_gUgfRei8af40eRFkOBXGpqjPIU0TltGumrTCvr0dnT4KB-7L75zDPQhdYphiwPx2My18Y9Z-mkGWTaEXxkdojDkRKceCHKMxEIBUgqAjdBbjBgAYZPIUjQjLKOOAx-hmFnax1VUS29CZtgs2aVzyNn95TZer5SpZ29aGpvS1DefoxOkq2ovDnaCP-cP77CldrB6fZ_eL1FAQbeokE0yWhmkGee6KUuRcUMko1g4wK7h2HFOQwAjkGFguHRWl05TK0nJJyARdD7mfofnqbGxV7aOxVaW3tumiyjjpA5ikvEfpgJrQxBisU5_B1zrsFAa1X0lt1LCS2q-koBfGve3q0NAVtS3_TL-z9MDdANj-z29vg4rG262xpQ_WtKps_P8NPwUldxU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2636145946</pqid></control><display><type>article</type><title>Crystal structure of SFPQ-NONO heterodimer</title><source>ScienceDirect Journals</source><creator>Schell, Bianca ; Legrand, Pierre ; Fribourg, Sébastien</creator><creatorcontrib>Schell, Bianca ; Legrand, Pierre ; Fribourg, Sébastien</creatorcontrib><description>The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous existence of six different dimeric complexes that sustain their function in many cellular processes such as pre-mRNA splicing, innate immunity, transcriptional regulation. In order to perform a complete structural analysis of all possible DBHS dimers, we have solved the crystal structure of the missing DBHS heterodimer SFPQ-NONO at 3.0 Å resolution. We identify subtle changes in amino acid composition and local secondary structure of the NOPS region orientation that may modulate affinity between complexes. Interestingly this area is found mutated in aggressive skin cancers and adenocarcinomas. -Structure of SFPQ-NONO heterodimer-Systematic structural analysis of all DBHS dimers-Identification of potential sites involved in fine-tuning dimer affinity</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2022.02.011</identifier><identifier>PMID: 35245601</identifier><language>eng</language><publisher>France: Elsevier B.V</publisher><subject>DBHS ; Heterodimer ; Paraspeckle ; Structure</subject><ispartof>Biochimie, 2022-07, Vol.198, p.1-7</ispartof><rights>2022 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)</rights><rights>Copyright © 2022 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933</citedby><cites>FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35245601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schell, Bianca</creatorcontrib><creatorcontrib>Legrand, Pierre</creatorcontrib><creatorcontrib>Fribourg, Sébastien</creatorcontrib><title>Crystal structure of SFPQ-NONO heterodimer</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous existence of six different dimeric complexes that sustain their function in many cellular processes such as pre-mRNA splicing, innate immunity, transcriptional regulation. In order to perform a complete structural analysis of all possible DBHS dimers, we have solved the crystal structure of the missing DBHS heterodimer SFPQ-NONO at 3.0 Å resolution. We identify subtle changes in amino acid composition and local secondary structure of the NOPS region orientation that may modulate affinity between complexes. Interestingly this area is found mutated in aggressive skin cancers and adenocarcinomas. -Structure of SFPQ-NONO heterodimer-Systematic structural analysis of all DBHS dimers-Identification of potential sites involved in fine-tuning dimer affinity</description><subject>DBHS</subject><subject>Heterodimer</subject><subject>Paraspeckle</subject><subject>Structure</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp9kF9LwzAUxYMobk6_gUgfRei8af40eRFkOBXGpqjPIU0TltGumrTCvr0dnT4KB-7L75zDPQhdYphiwPx2My18Y9Z-mkGWTaEXxkdojDkRKceCHKMxEIBUgqAjdBbjBgAYZPIUjQjLKOOAx-hmFnax1VUS29CZtgs2aVzyNn95TZer5SpZ29aGpvS1DefoxOkq2ovDnaCP-cP77CldrB6fZ_eL1FAQbeokE0yWhmkGee6KUuRcUMko1g4wK7h2HFOQwAjkGFguHRWl05TK0nJJyARdD7mfofnqbGxV7aOxVaW3tumiyjjpA5ikvEfpgJrQxBisU5_B1zrsFAa1X0lt1LCS2q-koBfGve3q0NAVtS3_TL-z9MDdANj-z29vg4rG262xpQ_WtKps_P8NPwUldxU</recordid><startdate>202207</startdate><enddate>202207</enddate><creator>Schell, Bianca</creator><creator>Legrand, Pierre</creator><creator>Fribourg, Sébastien</creator><general>Elsevier B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202207</creationdate><title>Crystal structure of SFPQ-NONO heterodimer</title><author>Schell, Bianca ; Legrand, Pierre ; Fribourg, Sébastien</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>DBHS</topic><topic>Heterodimer</topic><topic>Paraspeckle</topic><topic>Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schell, Bianca</creatorcontrib><creatorcontrib>Legrand, Pierre</creatorcontrib><creatorcontrib>Fribourg, Sébastien</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schell, Bianca</au><au>Legrand, Pierre</au><au>Fribourg, Sébastien</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of SFPQ-NONO heterodimer</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2022-07</date><risdate>2022</risdate><volume>198</volume><spage>1</spage><epage>7</epage><pages>1-7</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous existence of six different dimeric complexes that sustain their function in many cellular processes such as pre-mRNA splicing, innate immunity, transcriptional regulation. In order to perform a complete structural analysis of all possible DBHS dimers, we have solved the crystal structure of the missing DBHS heterodimer SFPQ-NONO at 3.0 Å resolution. We identify subtle changes in amino acid composition and local secondary structure of the NOPS region orientation that may modulate affinity between complexes. Interestingly this area is found mutated in aggressive skin cancers and adenocarcinomas. -Structure of SFPQ-NONO heterodimer-Systematic structural analysis of all DBHS dimers-Identification of potential sites involved in fine-tuning dimer affinity</abstract><cop>France</cop><pub>Elsevier B.V</pub><pmid>35245601</pmid><doi>10.1016/j.biochi.2022.02.011</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0300-9084
ispartof Biochimie, 2022-07, Vol.198, p.1-7
issn 0300-9084
1638-6183
language eng
recordid cdi_proquest_miscellaneous_2636145946
source ScienceDirect Journals
subjects DBHS
Heterodimer
Paraspeckle
Structure
title Crystal structure of SFPQ-NONO heterodimer
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T06%3A57%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structure%20of%20SFPQ-NONO%20heterodimer&rft.jtitle=Biochimie&rft.au=Schell,%20Bianca&rft.date=2022-07&rft.volume=198&rft.spage=1&rft.epage=7&rft.pages=1-7&rft.issn=0300-9084&rft.eissn=1638-6183&rft_id=info:doi/10.1016/j.biochi.2022.02.011&rft_dat=%3Cproquest_cross%3E2636145946%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c408t-f95859dc5a5077fbd876849541af015b6af614090530710579f48dfa449de6933%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2636145946&rft_id=info:pmid/35245601&rfr_iscdi=true