HMG1 Domains: The Victims of the Circumstances

The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Molecular biology (New York) 2002-05, Vol.36 (3), p.412
Hauptverfasser: Chikhirzhina, E V, Polyanichko, A M, Skvortsov, A N, Kostyleva, E I, Houssier, C, Vorob'ev, V I
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 3
container_start_page 412
container_title Molecular biology (New York)
container_volume 36
creator Chikhirzhina, E V
Polyanichko, A M
Skvortsov, A N
Kostyleva, E I
Houssier, C
Vorob'ev, V I
description The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1 was analyzed using recombinant protein HMG1-(A+B), which lacks the C-terminal amino acid sequence. The ψ-type CD spectra were common for DNA interaction with histone H1, but no spectra of this type were observed in HMG1-DNA systems even at high ionic strength. The CD spectrum of the truncated recombinant protein at high salt concentration somewhat resembled the ψ^sup +^-type spectrum. Two very intense positive bands were located near 215 nm and near 272 nm, and the whole CD spectrum was positive. The role of the C-terminal part of HMG1 in the formation of ordered DNA-protein complexes is discussed.[PUBLICATION ABSTRACT]
doi_str_mv 10.1023/A:1016019631909
format Article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_760103676</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2173802011</sourcerecordid><originalsourceid>FETCH-LOGICAL-c226t-63a713d9f8826473a6bdd4b44d5c73af5135424cbc32e9d8cd48cb02a933ceec3</originalsourceid><addsrcrecordid>eNotj81LwzAYxoM4sG6evQbvnW_ypmmy26huEyZepteRvkmxw7batP-_AYUHHn6X54OxewFrARIftxsBQoOwGoUFe8WyRCZHqYprlgFInRuLeMNuY7wAiCSZsfXhdS_409C5to8bfvoM_KOlqe0iHxo-JazakeYuTq6nEFds0bivGO7-fcned8-n6pAf3_Yv1faYk5R6yjW6UqC3jTFSqxKdrr1XtVK-oERNIbBQUlFNKIP1hrwyVIN0aSCFQLhkD3-53-PwM4c4nS_DPPap8lymj4C61PgLgl9DEg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>760103676</pqid></control><display><type>article</type><title>HMG1 Domains: The Victims of the Circumstances</title><source>SpringerLink Journals - AutoHoldings</source><creator>Chikhirzhina, E V ; Polyanichko, A M ; Skvortsov, A N ; Kostyleva, E I ; Houssier, C ; Vorob'ev, V I</creator><creatorcontrib>Chikhirzhina, E V ; Polyanichko, A M ; Skvortsov, A N ; Kostyleva, E I ; Houssier, C ; Vorob'ev, V I</creatorcontrib><description>The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1 was analyzed using recombinant protein HMG1-(A+B), which lacks the C-terminal amino acid sequence. The ψ-type CD spectra were common for DNA interaction with histone H1, but no spectra of this type were observed in HMG1-DNA systems even at high ionic strength. The CD spectrum of the truncated recombinant protein at high salt concentration somewhat resembled the ψ^sup +^-type spectrum. Two very intense positive bands were located near 215 nm and near 272 nm, and the whole CD spectrum was positive. The role of the C-terminal part of HMG1 in the formation of ordered DNA-protein complexes is discussed.[PUBLICATION ABSTRACT]</description><identifier>ISSN: 0026-8933</identifier><identifier>EISSN: 1608-3245</identifier><identifier>DOI: 10.1023/A:1016019631909</identifier><language>eng</language><publisher>New York: Springer Nature B.V</publisher><subject>Deoxyribonucleic acid ; DNA ; Proteins</subject><ispartof>Molecular biology (New York), 2002-05, Vol.36 (3), p.412</ispartof><rights>MAIK "Nauka/Interperiodica" 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c226t-63a713d9f8826473a6bdd4b44d5c73af5135424cbc32e9d8cd48cb02a933ceec3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Chikhirzhina, E V</creatorcontrib><creatorcontrib>Polyanichko, A M</creatorcontrib><creatorcontrib>Skvortsov, A N</creatorcontrib><creatorcontrib>Kostyleva, E I</creatorcontrib><creatorcontrib>Houssier, C</creatorcontrib><creatorcontrib>Vorob'ev, V I</creatorcontrib><title>HMG1 Domains: The Victims of the Circumstances</title><title>Molecular biology (New York)</title><description>The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1 was analyzed using recombinant protein HMG1-(A+B), which lacks the C-terminal amino acid sequence. The ψ-type CD spectra were common for DNA interaction with histone H1, but no spectra of this type were observed in HMG1-DNA systems even at high ionic strength. The CD spectrum of the truncated recombinant protein at high salt concentration somewhat resembled the ψ^sup +^-type spectrum. Two very intense positive bands were located near 215 nm and near 272 nm, and the whole CD spectrum was positive. The role of the C-terminal part of HMG1 in the formation of ordered DNA-protein complexes is discussed.[PUBLICATION ABSTRACT]</description><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Proteins</subject><issn>0026-8933</issn><issn>1608-3245</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNotj81LwzAYxoM4sG6evQbvnW_ypmmy26huEyZepteRvkmxw7batP-_AYUHHn6X54OxewFrARIftxsBQoOwGoUFe8WyRCZHqYprlgFInRuLeMNuY7wAiCSZsfXhdS_409C5to8bfvoM_KOlqe0iHxo-JazakeYuTq6nEFds0bivGO7-fcned8-n6pAf3_Yv1faYk5R6yjW6UqC3jTFSqxKdrr1XtVK-oERNIbBQUlFNKIP1hrwyVIN0aSCFQLhkD3-53-PwM4c4nS_DPPap8lymj4C61PgLgl9DEg</recordid><startdate>20020501</startdate><enddate>20020501</enddate><creator>Chikhirzhina, E V</creator><creator>Polyanichko, A M</creator><creator>Skvortsov, A N</creator><creator>Kostyleva, E I</creator><creator>Houssier, C</creator><creator>Vorob'ev, V I</creator><general>Springer Nature B.V</general><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20020501</creationdate><title>HMG1 Domains: The Victims of the Circumstances</title><author>Chikhirzhina, E V ; Polyanichko, A M ; Skvortsov, A N ; Kostyleva, E I ; Houssier, C ; Vorob'ev, V I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c226t-63a713d9f8826473a6bdd4b44d5c73af5135424cbc32e9d8cd48cb02a933ceec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chikhirzhina, E V</creatorcontrib><creatorcontrib>Polyanichko, A M</creatorcontrib><creatorcontrib>Skvortsov, A N</creatorcontrib><creatorcontrib>Kostyleva, E I</creatorcontrib><creatorcontrib>Houssier, C</creatorcontrib><creatorcontrib>Vorob'ev, V I</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><jtitle>Molecular biology (New York)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chikhirzhina, E V</au><au>Polyanichko, A M</au><au>Skvortsov, A N</au><au>Kostyleva, E I</au><au>Houssier, C</au><au>Vorob'ev, V I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HMG1 Domains: The Victims of the Circumstances</atitle><jtitle>Molecular biology (New York)</jtitle><date>2002-05-01</date><risdate>2002</risdate><volume>36</volume><issue>3</issue><spage>412</spage><pages>412-</pages><issn>0026-8933</issn><eissn>1608-3245</eissn><abstract>The method of circular dichroism (CD) was used to compare DNA behavior during its interaction with linker histone H1 and with nonhistone chromosomal protein HMG1 at different ionic strength and at different protein content in the system. The role of the negatively charged C-terminal segment of HMG1 was analyzed using recombinant protein HMG1-(A+B), which lacks the C-terminal amino acid sequence. The ψ-type CD spectra were common for DNA interaction with histone H1, but no spectra of this type were observed in HMG1-DNA systems even at high ionic strength. The CD spectrum of the truncated recombinant protein at high salt concentration somewhat resembled the ψ^sup +^-type spectrum. Two very intense positive bands were located near 215 nm and near 272 nm, and the whole CD spectrum was positive. The role of the C-terminal part of HMG1 in the formation of ordered DNA-protein complexes is discussed.[PUBLICATION ABSTRACT]</abstract><cop>New York</cop><pub>Springer Nature B.V</pub><doi>10.1023/A:1016019631909</doi></addata></record>
fulltext fulltext
identifier ISSN: 0026-8933
ispartof Molecular biology (New York), 2002-05, Vol.36 (3), p.412
issn 0026-8933
1608-3245
language eng
recordid cdi_proquest_journals_760103676
source SpringerLink Journals - AutoHoldings
subjects Deoxyribonucleic acid
DNA
Proteins
title HMG1 Domains: The Victims of the Circumstances
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T13%3A05%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=HMG1%20Domains:%20The%20Victims%20of%20the%20Circumstances&rft.jtitle=Molecular%20biology%20(New%20York)&rft.au=Chikhirzhina,%20E%20V&rft.date=2002-05-01&rft.volume=36&rft.issue=3&rft.spage=412&rft.pages=412-&rft.issn=0026-8933&rft.eissn=1608-3245&rft_id=info:doi/10.1023/A:1016019631909&rft_dat=%3Cproquest%3E2173802011%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=760103676&rft_id=info:pmid/&rfr_iscdi=true