Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis
Chromatin condenses several folds to form mitotic chromosomes during cell division and decondenses post-mitotically to reoccupy their nuclear territory and regain their specific transcriptional profile in a precisely lineage specific manner. This necessitates that the features of nuclear architectur...
Gespeichert in:
Veröffentlicht in: | Molecular & cellular proteomics 2018-10, Vol.17 (10), p.1965-1978 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1978 |
---|---|
container_issue | 10 |
container_start_page | 1965 |
container_title | Molecular & cellular proteomics |
container_volume | 17 |
creator | Sureka, Rahul Wadhwa, Rashi Thakur, Suman S. Pathak, Rashmi U. Mishra, Rakesh K. |
description | Chromatin condenses several folds to form mitotic chromosomes during cell division and decondenses post-mitotically to reoccupy their nuclear territory and regain their specific transcriptional profile in a precisely lineage specific manner. This necessitates that the features of nuclear architecture and DNA topology persist through mitosis. We compared the proteome of nuclease and high salt resistant fraction of interphase nucleus known as nuclear matrix (NuMat) and an equivalent biochemical fraction in the mitotic chromosome known as mitotic chromosome scaffold (MiCS). Our study elucidates that as much as 67% of the NuMat proteins are retained in the MiCS indicating that the features of nuclear architecture in interphase nucleus are retained on the mitotic chromosomes. Proteins of the NuMat/MiCS have large dynamic range of MS signal and were detected in sub-femtomolar amounts. Chromatin/RNA binding proteins with hydrolase and helicase activity are highly enriched in NuMat as well as MiCS. Although several transcription factors involved in functioning of interphase nucleus are present exclusively in NuMat, protein components responsible for assembly of membrane-less nuclear bodies are uniquely retained in MiCS. Our study clearly indicates that the features of nuclear architecture, in the structural context of NuMat, are retained in MiCS and possibly play an important role in maintenance of cell lineage specific transcriptional status during cell division and thereby, serve as components of cellular memory. |
doi_str_mv | 10.1074/mcp.RA118.000591 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6166678</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1535947620320387</els_id><sourcerecordid>2068346558</sourcerecordid><originalsourceid>FETCH-LOGICAL-c377t-b4634067c468b61c87f96ef27668665287040a51735f6e6597a88721d322e0d83</originalsourceid><addsrcrecordid>eNp1UctuFDEQtBCIPODOCfnIZRfbM34MB6RoIAQpIYgsZ8vr8ewaPPZgeyLgxEfwAXwbX4I3E1bhwKlb6uqq7ioAnmC0xIjXzwc9Lj-cYCyWCCHa4HvgENOKLppa1Pf3PWcH4CilTwgRhDl9CA5I0zSYIn4IfrVhGFW0KXgYevhu0s6oCC9UjvYrVL6DFzaHbDVstzEMIYXBwCut-j64Dr6PIRvrE7QevoplOG6tU_CKwNY4l37_-LmKyqfBpmRngTPl3KDi53RX7TJulLffVd6BVkVn2mxvdJNNj8CDXrlkHt_WY_Dx9PWqPVucX755256cL3TFeV6sa1bViHFdM7FmWAveN8z0hDMmGKNEcFQjRTGvaM8Mow1XQnCCu4oQgzpRHYOXM-84rQfTaeNzVE6O0ZZzv8mgrPx34u1WbsK1ZJgxxncEz24JYvgymZRleVsXG5Q3YUqSICaqmlG6g6IZqotnKZp-L4OR3AUrS7DyJlg5B1tWnt49b7_wN8kCeDEDTDHp2pook7bGa9PZaHSWXbD_Z_8Ddwe2pw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2068346558</pqid></control><display><type>article</type><title>Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis</title><source>PubMed (Medline)</source><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><source>EZB Electronic Journals Library</source><creator>Sureka, Rahul ; Wadhwa, Rashi ; Thakur, Suman S. ; Pathak, Rashmi U. ; Mishra, Rakesh K.</creator><creatorcontrib>Sureka, Rahul ; Wadhwa, Rashi ; Thakur, Suman S. ; Pathak, Rashmi U. ; Mishra, Rakesh K.</creatorcontrib><description>Chromatin condenses several folds to form mitotic chromosomes during cell division and decondenses post-mitotically to reoccupy their nuclear territory and regain their specific transcriptional profile in a precisely lineage specific manner. This necessitates that the features of nuclear architecture and DNA topology persist through mitosis. We compared the proteome of nuclease and high salt resistant fraction of interphase nucleus known as nuclear matrix (NuMat) and an equivalent biochemical fraction in the mitotic chromosome known as mitotic chromosome scaffold (MiCS). Our study elucidates that as much as 67% of the NuMat proteins are retained in the MiCS indicating that the features of nuclear architecture in interphase nucleus are retained on the mitotic chromosomes. Proteins of the NuMat/MiCS have large dynamic range of MS signal and were detected in sub-femtomolar amounts. Chromatin/RNA binding proteins with hydrolase and helicase activity are highly enriched in NuMat as well as MiCS. Although several transcription factors involved in functioning of interphase nucleus are present exclusively in NuMat, protein components responsible for assembly of membrane-less nuclear bodies are uniquely retained in MiCS. Our study clearly indicates that the features of nuclear architecture, in the structural context of NuMat, are retained in MiCS and possibly play an important role in maintenance of cell lineage specific transcriptional status during cell division and thereby, serve as components of cellular memory.</description><identifier>ISSN: 1535-9476</identifier><identifier>EISSN: 1535-9484</identifier><identifier>DOI: 10.1074/mcp.RA118.000591</identifier><identifier>PMID: 29991507</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell cycle ; Cellulra memory ; Chromatin function or biology ; Chromosomes - metabolism ; Drosophila ; Drosophila melanogaster - cytology ; Drosophila melanogaster - metabolism ; Drosophila S2 cell ; Electrophoresis, Gel, Two-Dimensional ; Gene Expression ; Mitosis ; Mitotic chromosome scaffold ; Nuclear Matrix ; Nuclear Matrix - metabolism ; Proteome - metabolism ; Quality Control ; Structural Biology ; Subcellular analysis ; Tandem Mass Spectrometry</subject><ispartof>Molecular & cellular proteomics, 2018-10, Vol.17 (10), p.1965-1978</ispartof><rights>2018 © 2018 Sureka et al.</rights><rights>2018 Sureka et al.</rights><rights>2018 Sureka et al. 2018 Sureka et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-b4634067c468b61c87f96ef27668665287040a51735f6e6597a88721d322e0d83</citedby><cites>FETCH-LOGICAL-c377t-b4634067c468b61c87f96ef27668665287040a51735f6e6597a88721d322e0d83</cites><orcidid>0000-0001-6636-7380</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6166678/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6166678/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29991507$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sureka, Rahul</creatorcontrib><creatorcontrib>Wadhwa, Rashi</creatorcontrib><creatorcontrib>Thakur, Suman S.</creatorcontrib><creatorcontrib>Pathak, Rashmi U.</creatorcontrib><creatorcontrib>Mishra, Rakesh K.</creatorcontrib><title>Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis</title><title>Molecular & cellular proteomics</title><addtitle>Mol Cell Proteomics</addtitle><description>Chromatin condenses several folds to form mitotic chromosomes during cell division and decondenses post-mitotically to reoccupy their nuclear territory and regain their specific transcriptional profile in a precisely lineage specific manner. This necessitates that the features of nuclear architecture and DNA topology persist through mitosis. We compared the proteome of nuclease and high salt resistant fraction of interphase nucleus known as nuclear matrix (NuMat) and an equivalent biochemical fraction in the mitotic chromosome known as mitotic chromosome scaffold (MiCS). Our study elucidates that as much as 67% of the NuMat proteins are retained in the MiCS indicating that the features of nuclear architecture in interphase nucleus are retained on the mitotic chromosomes. Proteins of the NuMat/MiCS have large dynamic range of MS signal and were detected in sub-femtomolar amounts. Chromatin/RNA binding proteins with hydrolase and helicase activity are highly enriched in NuMat as well as MiCS. Although several transcription factors involved in functioning of interphase nucleus are present exclusively in NuMat, protein components responsible for assembly of membrane-less nuclear bodies are uniquely retained in MiCS. Our study clearly indicates that the features of nuclear architecture, in the structural context of NuMat, are retained in MiCS and possibly play an important role in maintenance of cell lineage specific transcriptional status during cell division and thereby, serve as components of cellular memory.</description><subject>Animals</subject><subject>Cell cycle</subject><subject>Cellulra memory</subject><subject>Chromatin function or biology</subject><subject>Chromosomes - metabolism</subject><subject>Drosophila</subject><subject>Drosophila melanogaster - cytology</subject><subject>Drosophila melanogaster - metabolism</subject><subject>Drosophila S2 cell</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Gene Expression</subject><subject>Mitosis</subject><subject>Mitotic chromosome scaffold</subject><subject>Nuclear Matrix</subject><subject>Nuclear Matrix - metabolism</subject><subject>Proteome - metabolism</subject><subject>Quality Control</subject><subject>Structural Biology</subject><subject>Subcellular analysis</subject><subject>Tandem Mass Spectrometry</subject><issn>1535-9476</issn><issn>1535-9484</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1UctuFDEQtBCIPODOCfnIZRfbM34MB6RoIAQpIYgsZ8vr8ewaPPZgeyLgxEfwAXwbX4I3E1bhwKlb6uqq7ioAnmC0xIjXzwc9Lj-cYCyWCCHa4HvgENOKLppa1Pf3PWcH4CilTwgRhDl9CA5I0zSYIn4IfrVhGFW0KXgYevhu0s6oCC9UjvYrVL6DFzaHbDVstzEMIYXBwCut-j64Dr6PIRvrE7QevoplOG6tU_CKwNY4l37_-LmKyqfBpmRngTPl3KDi53RX7TJulLffVd6BVkVn2mxvdJNNj8CDXrlkHt_WY_Dx9PWqPVucX755256cL3TFeV6sa1bViHFdM7FmWAveN8z0hDMmGKNEcFQjRTGvaM8Mow1XQnCCu4oQgzpRHYOXM-84rQfTaeNzVE6O0ZZzv8mgrPx34u1WbsK1ZJgxxncEz24JYvgymZRleVsXG5Q3YUqSICaqmlG6g6IZqotnKZp-L4OR3AUrS7DyJlg5B1tWnt49b7_wN8kCeDEDTDHp2pook7bGa9PZaHSWXbD_Z_8Ddwe2pw</recordid><startdate>20181001</startdate><enddate>20181001</enddate><creator>Sureka, Rahul</creator><creator>Wadhwa, Rashi</creator><creator>Thakur, Suman S.</creator><creator>Pathak, Rashmi U.</creator><creator>Mishra, Rakesh K.</creator><general>Elsevier Inc</general><general>The American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-6636-7380</orcidid></search><sort><creationdate>20181001</creationdate><title>Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis</title><author>Sureka, Rahul ; Wadhwa, Rashi ; Thakur, Suman S. ; Pathak, Rashmi U. ; Mishra, Rakesh K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-b4634067c468b61c87f96ef27668665287040a51735f6e6597a88721d322e0d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Cell cycle</topic><topic>Cellulra memory</topic><topic>Chromatin function or biology</topic><topic>Chromosomes - metabolism</topic><topic>Drosophila</topic><topic>Drosophila melanogaster - cytology</topic><topic>Drosophila melanogaster - metabolism</topic><topic>Drosophila S2 cell</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Gene Expression</topic><topic>Mitosis</topic><topic>Mitotic chromosome scaffold</topic><topic>Nuclear Matrix</topic><topic>Nuclear Matrix - metabolism</topic><topic>Proteome - metabolism</topic><topic>Quality Control</topic><topic>Structural Biology</topic><topic>Subcellular analysis</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sureka, Rahul</creatorcontrib><creatorcontrib>Wadhwa, Rashi</creatorcontrib><creatorcontrib>Thakur, Suman S.</creatorcontrib><creatorcontrib>Pathak, Rashmi U.</creatorcontrib><creatorcontrib>Mishra, Rakesh K.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular & cellular proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sureka, Rahul</au><au>Wadhwa, Rashi</au><au>Thakur, Suman S.</au><au>Pathak, Rashmi U.</au><au>Mishra, Rakesh K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis</atitle><jtitle>Molecular & cellular proteomics</jtitle><addtitle>Mol Cell Proteomics</addtitle><date>2018-10-01</date><risdate>2018</risdate><volume>17</volume><issue>10</issue><spage>1965</spage><epage>1978</epage><pages>1965-1978</pages><issn>1535-9476</issn><eissn>1535-9484</eissn><abstract>Chromatin condenses several folds to form mitotic chromosomes during cell division and decondenses post-mitotically to reoccupy their nuclear territory and regain their specific transcriptional profile in a precisely lineage specific manner. This necessitates that the features of nuclear architecture and DNA topology persist through mitosis. We compared the proteome of nuclease and high salt resistant fraction of interphase nucleus known as nuclear matrix (NuMat) and an equivalent biochemical fraction in the mitotic chromosome known as mitotic chromosome scaffold (MiCS). Our study elucidates that as much as 67% of the NuMat proteins are retained in the MiCS indicating that the features of nuclear architecture in interphase nucleus are retained on the mitotic chromosomes. Proteins of the NuMat/MiCS have large dynamic range of MS signal and were detected in sub-femtomolar amounts. Chromatin/RNA binding proteins with hydrolase and helicase activity are highly enriched in NuMat as well as MiCS. Although several transcription factors involved in functioning of interphase nucleus are present exclusively in NuMat, protein components responsible for assembly of membrane-less nuclear bodies are uniquely retained in MiCS. Our study clearly indicates that the features of nuclear architecture, in the structural context of NuMat, are retained in MiCS and possibly play an important role in maintenance of cell lineage specific transcriptional status during cell division and thereby, serve as components of cellular memory.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>29991507</pmid><doi>10.1074/mcp.RA118.000591</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-6636-7380</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1535-9476 |
ispartof | Molecular & cellular proteomics, 2018-10, Vol.17 (10), p.1965-1978 |
issn | 1535-9476 1535-9484 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6166678 |
source | PubMed (Medline); MEDLINE; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; EZB Electronic Journals Library |
subjects | Animals Cell cycle Cellulra memory Chromatin function or biology Chromosomes - metabolism Drosophila Drosophila melanogaster - cytology Drosophila melanogaster - metabolism Drosophila S2 cell Electrophoresis, Gel, Two-Dimensional Gene Expression Mitosis Mitotic chromosome scaffold Nuclear Matrix Nuclear Matrix - metabolism Proteome - metabolism Quality Control Structural Biology Subcellular analysis Tandem Mass Spectrometry |
title | Comparison of Nuclear Matrix and Mitotic Chromosome Scaffold Proteins in Drosophila S2 Cells—Transmission of Hallmarks of Nuclear Organization Through Mitosis |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T11%3A12%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Comparison%20of%20Nuclear%20Matrix%20and%20Mitotic%20Chromosome%20Scaffold%20Proteins%20in%20Drosophila%20S2%20Cells%E2%80%94Transmission%20of%20Hallmarks%20of%20Nuclear%20Organization%20Through%20Mitosis&rft.jtitle=Molecular%20&%20cellular%20proteomics&rft.au=Sureka,%20Rahul&rft.date=2018-10-01&rft.volume=17&rft.issue=10&rft.spage=1965&rft.epage=1978&rft.pages=1965-1978&rft.issn=1535-9476&rft.eissn=1535-9484&rft_id=info:doi/10.1074/mcp.RA118.000591&rft_dat=%3Cproquest_pubme%3E2068346558%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2068346558&rft_id=info:pmid/29991507&rft_els_id=S1535947620320387&rfr_iscdi=true |