HARP Is an ATP-Driven Annealing Helicase

DNA-dependent adenosine triphosphatases (ATPases) participate in a broad range of biological processes including transcription, DNA repair, and chromatin dynamics. Mutations in the HepA-related protein (HARP) ATPase are responsible for Schimke immuno-osseous dysplasia (SIOD), but the function of the...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Science (American Association for the Advancement of Science) 2008-10, Vol.322 (5902), p.748-750
Hauptverfasser: Yusufzai, Timur, Kadonaga, James T
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 750
container_issue 5902
container_start_page 748
container_title Science (American Association for the Advancement of Science)
container_volume 322
creator Yusufzai, Timur
Kadonaga, James T
description DNA-dependent adenosine triphosphatases (ATPases) participate in a broad range of biological processes including transcription, DNA repair, and chromatin dynamics. Mutations in the HepA-related protein (HARP) ATPase are responsible for Schimke immuno-osseous dysplasia (SIOD), but the function of the protein is unknown. We found that HARP is an ATP-dependent annealing helicase that rewinds single-stranded DNA bubbles that are stably bound by replication protein A. Other related ATPases, including the DNA translocase Rad54, did not exhibit annealing helicase activity. Analysis of mutant HARP proteins suggests that SIOD is caused by a deficiency in annealing helicase activity. Moreover, the pleiotropy of HARP mutations is consistent with the function of HARP as an annealing helicase that acts throughout the genome to oppose the action of DNA-unwinding activities in the nucleus.
doi_str_mv 10.1126/science.1161233
format Article
fullrecord <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2587503</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>20145178</jstor_id><sourcerecordid>20145178</sourcerecordid><originalsourceid>FETCH-LOGICAL-c623t-da94f565e7e4c06103386899d65ea6bf20e8336698f972ea71e08808987d040b3</originalsourceid><addsrcrecordid>eNqFkU1vEzEQhi0EoiHlzAmIOEAv2449668LUlQKqVSpFbRny9nMBkcbb7GTSv33dZVVCxzakz-ex2OPX8becTjkXKij3ASKDZWF4gLxBRtxsLKyAvAlGwGgqgxoucfe5LwCKMzia7bHjdU1SjliB7Ppz4vJaZ74OJleXlTfUrihMo2RfBficjKjLjQ-0z571fou09thHLOr7yeXx7Pq7PzH6fH0rGqUwE218LZupZKkqW5AcUA0yli7KFtezVsBZBCVsqa1WpDXnMAYMNboBdQwxzH7uqt7vZ2vadFQ3CTfuesU1j7dut4H9y-J4bdb9jdOSKNluW7MvgwFUv9nS3nj1iE31HU-Ur_NrjQuUBuhi_n5SVNZjRZAPStyq7lFhCJ--k9c9dsUy385wVHeO7xIRzupSX3OidqH5ji4-1TdkKobUi0nPvz9J4_-EGMR3u-EVd706YEL4LXk2hT-ccdb3zu_TCG7q1-FludIKWtV4x2C0K2s</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>213593301</pqid></control><display><type>article</type><title>HARP Is an ATP-Driven Annealing Helicase</title><source>American Association for the Advancement of Science</source><source>Jstor Complete Legacy</source><source>MEDLINE</source><creator>Yusufzai, Timur ; Kadonaga, James T</creator><creatorcontrib>Yusufzai, Timur ; Kadonaga, James T</creatorcontrib><description>DNA-dependent adenosine triphosphatases (ATPases) participate in a broad range of biological processes including transcription, DNA repair, and chromatin dynamics. Mutations in the HepA-related protein (HARP) ATPase are responsible for Schimke immuno-osseous dysplasia (SIOD), but the function of the protein is unknown. We found that HARP is an ATP-dependent annealing helicase that rewinds single-stranded DNA bubbles that are stably bound by replication protein A. Other related ATPases, including the DNA translocase Rad54, did not exhibit annealing helicase activity. Analysis of mutant HARP proteins suggests that SIOD is caused by a deficiency in annealing helicase activity. Moreover, the pleiotropy of HARP mutations is consistent with the function of HARP as an annealing helicase that acts throughout the genome to oppose the action of DNA-unwinding activities in the nucleus.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1161233</identifier><identifier>PMID: 18974355</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Adenosine triphosphatase ; Adenosine triphosphatases ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - metabolism ; Adenosine Triphosphate - metabolism ; Annealing ; Deoxyribonucleic acid ; DNA ; DNA Helicases - chemistry ; DNA Helicases - deficiency ; DNA Helicases - genetics ; DNA Helicases - metabolism ; DNA, Single-Stranded - chemistry ; DNA, Single-Stranded - metabolism ; DNA-Binding Proteins ; Gels ; Genetic mutation ; Harps ; Humans ; Immunologic Deficiency Syndromes - genetics ; Molecular biology ; Mutant Proteins - metabolism ; Mutation ; Nuclear Proteins - metabolism ; Nucleic Acid Conformation ; Osteochondrodysplasias - genetics ; Plasmids ; Proteins ; Replication Protein A - metabolism ; Syndrome</subject><ispartof>Science (American Association for the Advancement of Science), 2008-10, Vol.322 (5902), p.748-750</ispartof><rights>Copyright 2008 American Association for the Advancement of Science</rights><rights>Copyright © 2008, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c623t-da94f565e7e4c06103386899d65ea6bf20e8336698f972ea71e08808987d040b3</citedby><cites>FETCH-LOGICAL-c623t-da94f565e7e4c06103386899d65ea6bf20e8336698f972ea71e08808987d040b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20145178$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20145178$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18974355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yusufzai, Timur</creatorcontrib><creatorcontrib>Kadonaga, James T</creatorcontrib><title>HARP Is an ATP-Driven Annealing Helicase</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>DNA-dependent adenosine triphosphatases (ATPases) participate in a broad range of biological processes including transcription, DNA repair, and chromatin dynamics. Mutations in the HepA-related protein (HARP) ATPase are responsible for Schimke immuno-osseous dysplasia (SIOD), but the function of the protein is unknown. We found that HARP is an ATP-dependent annealing helicase that rewinds single-stranded DNA bubbles that are stably bound by replication protein A. Other related ATPases, including the DNA translocase Rad54, did not exhibit annealing helicase activity. Analysis of mutant HARP proteins suggests that SIOD is caused by a deficiency in annealing helicase activity. Moreover, the pleiotropy of HARP mutations is consistent with the function of HARP as an annealing helicase that acts throughout the genome to oppose the action of DNA-unwinding activities in the nucleus.</description><subject>Adenosine triphosphatase</subject><subject>Adenosine triphosphatases</subject><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Annealing</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Helicases - chemistry</subject><subject>DNA Helicases - deficiency</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - metabolism</subject><subject>DNA, Single-Stranded - chemistry</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>DNA-Binding Proteins</subject><subject>Gels</subject><subject>Genetic mutation</subject><subject>Harps</subject><subject>Humans</subject><subject>Immunologic Deficiency Syndromes - genetics</subject><subject>Molecular biology</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nucleic Acid Conformation</subject><subject>Osteochondrodysplasias - genetics</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Replication Protein A - metabolism</subject><subject>Syndrome</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0EoiHlzAmIOEAv2449668LUlQKqVSpFbRny9nMBkcbb7GTSv33dZVVCxzakz-ex2OPX8becTjkXKij3ASKDZWF4gLxBRtxsLKyAvAlGwGgqgxoucfe5LwCKMzia7bHjdU1SjliB7Ppz4vJaZ74OJleXlTfUrihMo2RfBficjKjLjQ-0z571fou09thHLOr7yeXx7Pq7PzH6fH0rGqUwE218LZupZKkqW5AcUA0yli7KFtezVsBZBCVsqa1WpDXnMAYMNboBdQwxzH7uqt7vZ2vadFQ3CTfuesU1j7dut4H9y-J4bdb9jdOSKNluW7MvgwFUv9nS3nj1iE31HU-Ur_NrjQuUBuhi_n5SVNZjRZAPStyq7lFhCJ--k9c9dsUy385wVHeO7xIRzupSX3OidqH5ji4-1TdkKobUi0nPvz9J4_-EGMR3u-EVd706YEL4LXk2hT-ccdb3zu_TCG7q1-FludIKWtV4x2C0K2s</recordid><startdate>20081031</startdate><enddate>20081031</enddate><creator>Yusufzai, Timur</creator><creator>Kadonaga, James T</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>FBQ</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20081031</creationdate><title>HARP Is an ATP-Driven Annealing Helicase</title><author>Yusufzai, Timur ; Kadonaga, James T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c623t-da94f565e7e4c06103386899d65ea6bf20e8336698f972ea71e08808987d040b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adenosine triphosphatase</topic><topic>Adenosine triphosphatases</topic><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Annealing</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Helicases - chemistry</topic><topic>DNA Helicases - deficiency</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - metabolism</topic><topic>DNA, Single-Stranded - chemistry</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>DNA-Binding Proteins</topic><topic>Gels</topic><topic>Genetic mutation</topic><topic>Harps</topic><topic>Humans</topic><topic>Immunologic Deficiency Syndromes - genetics</topic><topic>Molecular biology</topic><topic>Mutant Proteins - metabolism</topic><topic>Mutation</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nucleic Acid Conformation</topic><topic>Osteochondrodysplasias - genetics</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Replication Protein A - metabolism</topic><topic>Syndrome</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yusufzai, Timur</creatorcontrib><creatorcontrib>Kadonaga, James T</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yusufzai, Timur</au><au>Kadonaga, James T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HARP Is an ATP-Driven Annealing Helicase</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2008-10-31</date><risdate>2008</risdate><volume>322</volume><issue>5902</issue><spage>748</spage><epage>750</epage><pages>748-750</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>DNA-dependent adenosine triphosphatases (ATPases) participate in a broad range of biological processes including transcription, DNA repair, and chromatin dynamics. Mutations in the HepA-related protein (HARP) ATPase are responsible for Schimke immuno-osseous dysplasia (SIOD), but the function of the protein is unknown. We found that HARP is an ATP-dependent annealing helicase that rewinds single-stranded DNA bubbles that are stably bound by replication protein A. Other related ATPases, including the DNA translocase Rad54, did not exhibit annealing helicase activity. Analysis of mutant HARP proteins suggests that SIOD is caused by a deficiency in annealing helicase activity. Moreover, the pleiotropy of HARP mutations is consistent with the function of HARP as an annealing helicase that acts throughout the genome to oppose the action of DNA-unwinding activities in the nucleus.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>18974355</pmid><doi>10.1126/science.1161233</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0036-8075
ispartof Science (American Association for the Advancement of Science), 2008-10, Vol.322 (5902), p.748-750
issn 0036-8075
1095-9203
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2587503
source American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE
subjects Adenosine triphosphatase
Adenosine triphosphatases
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Annealing
Deoxyribonucleic acid
DNA
DNA Helicases - chemistry
DNA Helicases - deficiency
DNA Helicases - genetics
DNA Helicases - metabolism
DNA, Single-Stranded - chemistry
DNA, Single-Stranded - metabolism
DNA-Binding Proteins
Gels
Genetic mutation
Harps
Humans
Immunologic Deficiency Syndromes - genetics
Molecular biology
Mutant Proteins - metabolism
Mutation
Nuclear Proteins - metabolism
Nucleic Acid Conformation
Osteochondrodysplasias - genetics
Plasmids
Proteins
Replication Protein A - metabolism
Syndrome
title HARP Is an ATP-Driven Annealing Helicase
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-14T01%3A29%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=HARP%20Is%20an%20ATP-Driven%20Annealing%20Helicase&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Yusufzai,%20Timur&rft.date=2008-10-31&rft.volume=322&rft.issue=5902&rft.spage=748&rft.epage=750&rft.pages=748-750&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1161233&rft_dat=%3Cjstor_pubme%3E20145178%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213593301&rft_id=info:pmid/18974355&rft_jstor_id=20145178&rfr_iscdi=true