Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin
Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chr...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1990-11, Vol.265 (33), p.20077-20080 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 20080 |
|---|---|
| container_issue | 33 |
| container_start_page | 20077 |
| container_title | The Journal of biological chemistry |
| container_volume | 265 |
| creator | Bustin, M Crippa, M P Pash, J M |
| description | Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chromatin. Competitive enzyme-linked immunosorbent assays indicate that the central region of the proteins, which contains their DNA binding domain and is positively charged, is exposed to a smaller degree than the C-terminal region of the proteins, which has a net negative charge. The C-terminal regions of the HMG-14 and HMG-17 proteins are exposed and available to interact with other proteins. |
| doi_str_mv | 10.1016/S0021-9258(17)30469-6 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16509202</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925817304696</els_id><sourcerecordid>16509202</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4486-d5ab68974c4d67c3fabe16da0ba2b1382c0a90663b889b78dee2ee4c6326decf3</originalsourceid><addsrcrecordid>eNqFkEtr3TAQRkVoSG-T_ISAFqW0C6d6WbJXJYQ-AoEs0kB2Qo9xrGBbt5Ld5v776D7IttoIac43MxyELii5pITKr_eEMFq1rG4-U_WFEyHbSh6hFSUNr3hNH9-h1RvyHn3I-ZmUI1p6gk4YE5yodoW6m3Fcpuh6GIMzAzaTGTY5ZBw7PPeA4WUd85Jg--7DU4_HaMMQ5g1-SnFZ43WKM4QJU1GiHlOFC90ZBxmXX9enOJo5TGfouDNDhvPDfYoefnz_ff2rur37eXN9dVs5IRpZ-dpY2bRKOOGlcrwzFqj0hljDLOUNc8S0REpum6a1qvEADEA4yZn04Dp-ij7t-5a9_iyQZz2G7GAYzARxyZrKmrSMsALWe9ClmHOCTq9TGE3aaEr01q_e-dVbeZoqvfOrZcldHAYsdgT_ljoILfWP-_pW1r-QQNuws6uZrDXnmhGiVMG-7TEoMv4GSDq7AJMDXyJu1j6G_yzyCqHHlwg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16509202</pqid></control><display><type>article</type><title>Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Bustin, M ; Crippa, M P ; Pash, J M</creator><creatorcontrib>Bustin, M ; Crippa, M P ; Pash, J M</creatorcontrib><description>Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chromatin. Competitive enzyme-linked immunosorbent assays indicate that the central region of the proteins, which contains their DNA binding domain and is positively charged, is exposed to a smaller degree than the C-terminal region of the proteins, which has a net negative charge. The C-terminal regions of the HMG-14 and HMG-17 proteins are exposed and available to interact with other proteins.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)30469-6</identifier><identifier>PMID: 2243079</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Antigen-Antibody Complex ; Binding, Competitive ; Cell Nucleus - ultrastructure ; Chickens ; Chromatin - chemistry ; Chromatin - ultrastructure ; Enzyme-Linked Immunosorbent Assay ; Erythrocytes - chemistry ; HeLa Cells - chemistry ; High Mobility Group Proteins - analysis ; High Mobility Group Proteins - immunology ; High Mobility Group Proteins - ultrastructure ; Histones - ultrastructure ; Humans ; Immune Sera ; Models, Structural ; Molecular Sequence Data ; Nucleosomes - ultrastructure ; Peptides - chemical synthesis ; Protein Conformation</subject><ispartof>The Journal of biological chemistry, 1990-11, Vol.265 (33), p.20077-20080</ispartof><rights>1990 © 1990 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4486-d5ab68974c4d67c3fabe16da0ba2b1382c0a90663b889b78dee2ee4c6326decf3</citedby><cites>FETCH-LOGICAL-c4486-d5ab68974c4d67c3fabe16da0ba2b1382c0a90663b889b78dee2ee4c6326decf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2243079$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bustin, M</creatorcontrib><creatorcontrib>Crippa, M P</creatorcontrib><creatorcontrib>Pash, J M</creatorcontrib><title>Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chromatin. Competitive enzyme-linked immunosorbent assays indicate that the central region of the proteins, which contains their DNA binding domain and is positively charged, is exposed to a smaller degree than the C-terminal region of the proteins, which has a net negative charge. The C-terminal regions of the HMG-14 and HMG-17 proteins are exposed and available to interact with other proteins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigen-Antibody Complex</subject><subject>Binding, Competitive</subject><subject>Cell Nucleus - ultrastructure</subject><subject>Chickens</subject><subject>Chromatin - chemistry</subject><subject>Chromatin - ultrastructure</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Erythrocytes - chemistry</subject><subject>HeLa Cells - chemistry</subject><subject>High Mobility Group Proteins - analysis</subject><subject>High Mobility Group Proteins - immunology</subject><subject>High Mobility Group Proteins - ultrastructure</subject><subject>Histones - ultrastructure</subject><subject>Humans</subject><subject>Immune Sera</subject><subject>Models, Structural</subject><subject>Molecular Sequence Data</subject><subject>Nucleosomes - ultrastructure</subject><subject>Peptides - chemical synthesis</subject><subject>Protein Conformation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtr3TAQRkVoSG-T_ISAFqW0C6d6WbJXJYQ-AoEs0kB2Qo9xrGBbt5Ld5v776D7IttoIac43MxyELii5pITKr_eEMFq1rG4-U_WFEyHbSh6hFSUNr3hNH9-h1RvyHn3I-ZmUI1p6gk4YE5yodoW6m3Fcpuh6GIMzAzaTGTY5ZBw7PPeA4WUd85Jg--7DU4_HaMMQ5g1-SnFZ43WKM4QJU1GiHlOFC90ZBxmXX9enOJo5TGfouDNDhvPDfYoefnz_ff2rur37eXN9dVs5IRpZ-dpY2bRKOOGlcrwzFqj0hljDLOUNc8S0REpum6a1qvEADEA4yZn04Dp-ij7t-5a9_iyQZz2G7GAYzARxyZrKmrSMsALWe9ClmHOCTq9TGE3aaEr01q_e-dVbeZoqvfOrZcldHAYsdgT_ljoILfWP-_pW1r-QQNuws6uZrDXnmhGiVMG-7TEoMv4GSDq7AJMDXyJu1j6G_yzyCqHHlwg</recordid><startdate>19901125</startdate><enddate>19901125</enddate><creator>Bustin, M</creator><creator>Crippa, M P</creator><creator>Pash, J M</creator><general>Elsevier Inc</general><general>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>7TM</scope></search><sort><creationdate>19901125</creationdate><title>Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin</title><author>Bustin, M ; Crippa, M P ; Pash, J M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4486-d5ab68974c4d67c3fabe16da0ba2b1382c0a90663b889b78dee2ee4c6326decf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigen-Antibody Complex</topic><topic>Binding, Competitive</topic><topic>Cell Nucleus - ultrastructure</topic><topic>Chickens</topic><topic>Chromatin - chemistry</topic><topic>Chromatin - ultrastructure</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Erythrocytes - chemistry</topic><topic>HeLa Cells - chemistry</topic><topic>High Mobility Group Proteins - analysis</topic><topic>High Mobility Group Proteins - immunology</topic><topic>High Mobility Group Proteins - ultrastructure</topic><topic>Histones - ultrastructure</topic><topic>Humans</topic><topic>Immune Sera</topic><topic>Models, Structural</topic><topic>Molecular Sequence Data</topic><topic>Nucleosomes - ultrastructure</topic><topic>Peptides - chemical synthesis</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bustin, M</creatorcontrib><creatorcontrib>Crippa, M P</creatorcontrib><creatorcontrib>Pash, J M</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>Nucleic Acids Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bustin, M</au><au>Crippa, M P</au><au>Pash, J M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-11-25</date><risdate>1990</risdate><volume>265</volume><issue>33</issue><spage>20077</spage><epage>20080</epage><pages>20077-20080</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Antisera were elicited against synthetic peptides corresponding either to regions common to all members of the high mobility group 14 and 17 protein family protein or to distinct domains of the HMG-14 or HMG-17 subgroup. The antisera were used to probe the accessibility of various HMG domains in chromatin. Competitive enzyme-linked immunosorbent assays indicate that the central region of the proteins, which contains their DNA binding domain and is positively charged, is exposed to a smaller degree than the C-terminal region of the proteins, which has a net negative charge. The C-terminal regions of the HMG-14 and HMG-17 proteins are exposed and available to interact with other proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>2243079</pmid><doi>10.1016/S0021-9258(17)30469-6</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1990-11, Vol.265 (33), p.20077-20080 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16509202 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Antigen-Antibody Complex Binding, Competitive Cell Nucleus - ultrastructure Chickens Chromatin - chemistry Chromatin - ultrastructure Enzyme-Linked Immunosorbent Assay Erythrocytes - chemistry HeLa Cells - chemistry High Mobility Group Proteins - analysis High Mobility Group Proteins - immunology High Mobility Group Proteins - ultrastructure Histones - ultrastructure Humans Immune Sera Models, Structural Molecular Sequence Data Nucleosomes - ultrastructure Peptides - chemical synthesis Protein Conformation |
| title | Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T21%3A47%3A40IST&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=Immunochemical%20analysis%20of%20the%20exposure%20of%20high%20mobility%20group%20protein%2014%20and%2017%20surfaces%20in%20chromatin&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Bustin,%20M&rft.date=1990-11-25&rft.volume=265&rft.issue=33&rft.spage=20077&rft.epage=20080&rft.pages=20077-20080&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(17)30469-6&rft_dat=%3Cproquest_cross%3E16509202%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16509202&rft_id=info:pmid/2243079&rft_els_id=S0021925817304696&rfr_iscdi=true |