Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins
Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the herpes simplex virus type-1 initiator protein (UL9)...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2002-02, Vol.277 (7), p.5660-5666 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5666 |
|---|---|
| container_issue | 7 |
| container_start_page | 5660 |
| container_title | The Journal of biological chemistry |
| container_volume | 277 |
| creator | Tanguy Le Gac, Nicolas Boehmer, Paul E |
| description | Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of
initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the
herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the viral origins of replication. Hsp40 and Hsp70 act
substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this effect is Hsp40. Heat shock
proteins also stimulate the ATPase activity of UL9 with oriS and increase opening of the origin. In contrast, heat shock proteins
have no effect on the origin-independent activities of UL9 suggesting that their role is not merely in refolding denatured
protein. These observations are consistent with a role for heat shock proteins in activating UL9 to efficiently initiate viral
origin-dependent DNA replication. The action of heat shock proteins in this capacity is analogous to their role in activating
the initiator proteins of other organisms. |
| doi_str_mv | 10.1074/jbc.M108316200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_18255987</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18255987</sourcerecordid><originalsourceid>FETCH-LOGICAL-c389t-55fa48b7467aa575bc7f2853a799727bce29d8bc66eb02ce495b32275fcd57ca3</originalsourceid><addsrcrecordid>eNpFkE1LAzEQhoMoWqtXjxI8iB62JtnNZnMsRa1QUbCKt5Cks91o98Nkq_bfu6WVzmUG5nnfw4PQGSUDSkRy82Hs4JGSLKYpI2QP9dZ3FHP6vo96hDAaScazI3QcwgfpJpH0EB1RKijlcdpDemhb961bV1e4znFbAB6DbyDgF1c2C_jFb84vA56uGogofvJu7qrIuGrmqjl-9nULrsJXrxN5jc2qy-oWvxS1_fz_hRN0kOtFgNPt7qPXu9vpaBxNnu4fRsNJZONMthHnuU4yI5JUaM0FN1bkLOOxFlIKJowFJmeZsWkKhjALieQmZkzw3M64sDruo8tNb-PrryWEVpUuWFgsdAX1MiiaMc5lJjpwsAGtr0PwkKvGu1L7laJEraWqTqraSe0C59vmpSlhtsO3FjvgYgMUbl78OA_KuNoWUComhBKKpymJ_wAxUn0l</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18255987</pqid></control><display><type>article</type><title>Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Tanguy Le Gac, Nicolas ; Boehmer, Paul E</creator><creatorcontrib>Tanguy Le Gac, Nicolas ; Boehmer, Paul E</creatorcontrib><description>Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of
initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the
herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the viral origins of replication. Hsp40 and Hsp70 act
substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this effect is Hsp40. Heat shock
proteins also stimulate the ATPase activity of UL9 with oriS and increase opening of the origin. In contrast, heat shock proteins
have no effect on the origin-independent activities of UL9 suggesting that their role is not merely in refolding denatured
protein. These observations are consistent with a role for heat shock proteins in activating UL9 to efficiently initiate viral
origin-dependent DNA replication. The action of heat shock proteins in this capacity is analogous to their role in activating
the initiator proteins of other organisms.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M108316200</identifier><identifier>PMID: 11711536</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphatases - metabolism ; DNA Helicases - metabolism ; DNA-Binding Proteins - metabolism ; Dose-Response Relationship, Drug ; Escherichia coli - metabolism ; Heat-Shock Proteins - metabolism ; Herpes simplex virus 1 ; HSP40 Heat-Shock Proteins ; Hsp40 protein ; HSP70 Heat-Shock Proteins - metabolism ; Humans ; Hydrolysis ; Kinetics ; Potassium Permanganate - pharmacology ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins - metabolism ; Time Factors ; UL9 protein ; Viral Proteins - metabolism</subject><ispartof>The Journal of biological chemistry, 2002-02, Vol.277 (7), p.5660-5666</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-55fa48b7467aa575bc7f2853a799727bce29d8bc66eb02ce495b32275fcd57ca3</citedby><cites>FETCH-LOGICAL-c389t-55fa48b7467aa575bc7f2853a799727bce29d8bc66eb02ce495b32275fcd57ca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27933,27934</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11711536$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanguy Le Gac, Nicolas</creatorcontrib><creatorcontrib>Boehmer, Paul E</creatorcontrib><title>Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of
initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the
herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the viral origins of replication. Hsp40 and Hsp70 act
substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this effect is Hsp40. Heat shock
proteins also stimulate the ATPase activity of UL9 with oriS and increase opening of the origin. In contrast, heat shock proteins
have no effect on the origin-independent activities of UL9 suggesting that their role is not merely in refolding denatured
protein. These observations are consistent with a role for heat shock proteins in activating UL9 to efficiently initiate viral
origin-dependent DNA replication. The action of heat shock proteins in this capacity is analogous to their role in activating
the initiator proteins of other organisms.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>DNA Helicases - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Escherichia coli - metabolism</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Herpes simplex virus 1</subject><subject>HSP40 Heat-Shock Proteins</subject><subject>Hsp40 protein</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Potassium Permanganate - pharmacology</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - metabolism</subject><subject>Time Factors</subject><subject>UL9 protein</subject><subject>Viral Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1LAzEQhoMoWqtXjxI8iB62JtnNZnMsRa1QUbCKt5Cks91o98Nkq_bfu6WVzmUG5nnfw4PQGSUDSkRy82Hs4JGSLKYpI2QP9dZ3FHP6vo96hDAaScazI3QcwgfpJpH0EB1RKijlcdpDemhb961bV1e4znFbAB6DbyDgF1c2C_jFb84vA56uGogofvJu7qrIuGrmqjl-9nULrsJXrxN5jc2qy-oWvxS1_fz_hRN0kOtFgNPt7qPXu9vpaBxNnu4fRsNJZONMthHnuU4yI5JUaM0FN1bkLOOxFlIKJowFJmeZsWkKhjALieQmZkzw3M64sDruo8tNb-PrryWEVpUuWFgsdAX1MiiaMc5lJjpwsAGtr0PwkKvGu1L7laJEraWqTqraSe0C59vmpSlhtsO3FjvgYgMUbl78OA_KuNoWUComhBKKpymJ_wAxUn0l</recordid><startdate>20020215</startdate><enddate>20020215</enddate><creator>Tanguy Le Gac, Nicolas</creator><creator>Boehmer, Paul E</creator><general>American Society for Biochemistry and Molecular Biology</general><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><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20020215</creationdate><title>Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins</title><author>Tanguy Le Gac, Nicolas ; Boehmer, Paul E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-55fa48b7467aa575bc7f2853a799727bce29d8bc66eb02ce495b32275fcd57ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>DNA Helicases - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Escherichia coli - metabolism</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Herpes simplex virus 1</topic><topic>HSP40 Heat-Shock Proteins</topic><topic>Hsp40 protein</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Potassium Permanganate - pharmacology</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - metabolism</topic><topic>Time Factors</topic><topic>UL9 protein</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanguy Le Gac, Nicolas</creatorcontrib><creatorcontrib>Boehmer, Paul E</creatorcontrib><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><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanguy Le Gac, Nicolas</au><au>Boehmer, Paul E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-02-15</date><risdate>2002</risdate><volume>277</volume><issue>7</issue><spage>5660</spage><epage>5666</epage><pages>5660-5666</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of
initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the
herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the viral origins of replication. Hsp40 and Hsp70 act
substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this effect is Hsp40. Heat shock
proteins also stimulate the ATPase activity of UL9 with oriS and increase opening of the origin. In contrast, heat shock proteins
have no effect on the origin-independent activities of UL9 suggesting that their role is not merely in refolding denatured
protein. These observations are consistent with a role for heat shock proteins in activating UL9 to efficiently initiate viral
origin-dependent DNA replication. The action of heat shock proteins in this capacity is analogous to their role in activating
the initiator proteins of other organisms.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>11711536</pmid><doi>10.1074/jbc.M108316200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2002-02, Vol.277 (7), p.5660-5666 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_18255987 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - metabolism DNA Helicases - metabolism DNA-Binding Proteins - metabolism Dose-Response Relationship, Drug Escherichia coli - metabolism Heat-Shock Proteins - metabolism Herpes simplex virus 1 HSP40 Heat-Shock Proteins Hsp40 protein HSP70 Heat-Shock Proteins - metabolism Humans Hydrolysis Kinetics Potassium Permanganate - pharmacology Protein Binding Protein Structure, Tertiary Recombinant Proteins - metabolism Time Factors UL9 protein Viral Proteins - metabolism |
| title | Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-02T06%3A36%3A19IST&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=Activation%20of%20the%20Herpes%20Simplex%20Virus%20Type-1%20Origin-binding%20Protein%20(UL9)%20by%20Heat%20Shock%20Proteins&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Tanguy%20Le%20Gac,%20Nicolas&rft.date=2002-02-15&rft.volume=277&rft.issue=7&rft.spage=5660&rft.epage=5666&rft.pages=5660-5666&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M108316200&rft_dat=%3Cproquest_cross%3E18255987%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=18255987&rft_id=info:pmid/11711536&rfr_iscdi=true |