Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex
Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the Drosophila melanogaster origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ do...
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| Veröffentlicht in: | Nature structural & molecular biology 2006-08, Vol.13 (8), p.684-690 |
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| creator | Clarey, Megan G Erzberger, Jan P Grob, Patricia Leschziner, Andres E Berger, James M Nogales, Eva Botchan, Michael |
| description | Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the
Drosophila melanogaster
origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ domains in ORC contain a conserved structural element that, in DnaA, promotes formation of a right-handed helix, indicating that helical AAA+ substructures may be a feature of all initiators. A DnaA helical pentamer can be docked into ORC, and the location of Orc5 uniquely positions this core. The results suggest that ATP-dependent conformational changes observed in ORC derive from reorientation of the AAA+ domains. By analogy to the DNA-wrapping activity of DnaA, we posit that ORC together with Cdc6 prepares origin DNA for helicase loading through mechanisms related to the established pathway of prokaryotes. |
| doi_str_mv | 10.1038/nsmb1121 |
| format | Article |
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Drosophila melanogaster
origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ domains in ORC contain a conserved structural element that, in DnaA, promotes formation of a right-handed helix, indicating that helical AAA+ substructures may be a feature of all initiators. A DnaA helical pentamer can be docked into ORC, and the location of Orc5 uniquely positions this core. The results suggest that ATP-dependent conformational changes observed in ORC derive from reorientation of the AAA+ domains. By analogy to the DNA-wrapping activity of DnaA, we posit that ORC together with Cdc6 prepares origin DNA for helicase loading through mechanisms related to the established pathway of prokaryotes.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb1121</identifier><identifier>PMID: 16829958</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adenosine triphosphatase ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Animals ; ATP ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Binding proteins ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; Deoxyribonucleic acid ; DNA ; DNA replication ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Drosophila melanogaster ; Drosophila Proteins - chemistry ; Drosophila Proteins - metabolism ; Life Sciences ; Membrane Biology ; Microscopy, Electron ; Models, Molecular ; Molecular biology ; Molecular Sequence Data ; Molecular structure ; Nucleotides ; Nucleotides - metabolism ; Origin Recognition Complex - chemistry ; Origin Recognition Complex - metabolism ; Physiological aspects ; Protein Conformation ; Protein Structure ; Proteins ; Sequence Homology, Amino Acid</subject><ispartof>Nature structural & molecular biology, 2006-08, Vol.13 (8), p.684-690</ispartof><rights>Springer Nature America, Inc. 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Aug 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-8de97432e611f261034664caa205c764ad8b8b24c454a23193d60d94982dffa43</citedby><cites>FETCH-LOGICAL-c474t-8de97432e611f261034664caa205c764ad8b8b24c454a23193d60d94982dffa43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb1121$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb1121$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16829958$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clarey, Megan G</creatorcontrib><creatorcontrib>Erzberger, Jan P</creatorcontrib><creatorcontrib>Grob, Patricia</creatorcontrib><creatorcontrib>Leschziner, Andres E</creatorcontrib><creatorcontrib>Berger, James M</creatorcontrib><creatorcontrib>Nogales, Eva</creatorcontrib><creatorcontrib>Botchan, Michael</creatorcontrib><title>Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the
Drosophila melanogaster
origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ domains in ORC contain a conserved structural element that, in DnaA, promotes formation of a right-handed helix, indicating that helical AAA+ substructures may be a feature of all initiators. A DnaA helical pentamer can be docked into ORC, and the location of Orc5 uniquely positions this core. The results suggest that ATP-dependent conformational changes observed in ORC derive from reorientation of the AAA+ domains. By analogy to the DNA-wrapping activity of DnaA, we posit that ORC together with Cdc6 prepares origin DNA for helicase loading through mechanisms related to the established pathway of prokaryotes.</description><subject>Adenosine triphosphatase</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>ATP</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding proteins</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA replication</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins - chemistry</subject><subject>Drosophila Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Nucleotides</subject><subject>Nucleotides - metabolism</subject><subject>Origin Recognition Complex - chemistry</subject><subject>Origin Recognition Complex - metabolism</subject><subject>Physiological aspects</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Proteins</subject><subject>Sequence Homology, Amino Acid</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkl1rFDEUhgex2FoFf4EMCmIvpk4-J7lcarWFouDHdcgmZ6apM8k2yUD99826a5dVQXKRcM5z3sN5c6rqBWpPUUvEO5-mJUIYPaqOEKOskVKwxw9vSQ6rpyndtC1mrCNPqkPEBZaSiaPKfJrNCCE7C42FFXgLPtcm-D7ESWcXvB5rc639AKl2vs7XUL_3etGM7gcULkId-l_REN1QgAgmDN6tK0t6Wo1w96w66PWY4Pn2Pq6-fzj_dnbRXH3-eHm2uGoM7WhuhAXZUYKBI9RjXgajnFOjNW6Z6TjVVizFElNDGdWYIEksb62kUmDb95qS4-rNRncVw-0MKavJJQPjqD2EOSkuOtSyrvsvWKQRb7Es4Ks_wJswx2JJUhgL3BGCUIFeb6BBj6BccS5HbdaKaoEEI50Ukhfq9B9UORYmV_yG3pX4XsHJXkFhMtzlQc8pqcuvX_bZtxvWxJBShF6topt0_KlQq9Ybon5vSEFfbkealxPYHbhdiV3fVFLl2-Nu5r_E7gHu5MGA</recordid><startdate>20060801</startdate><enddate>20060801</enddate><creator>Clarey, Megan G</creator><creator>Erzberger, Jan P</creator><creator>Grob, Patricia</creator><creator>Leschziner, Andres E</creator><creator>Berger, James M</creator><creator>Nogales, Eva</creator><creator>Botchan, Michael</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7SS</scope><scope>7X8</scope></search><sort><creationdate>20060801</creationdate><title>Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex</title><author>Clarey, Megan G ; Erzberger, Jan P ; Grob, Patricia ; Leschziner, Andres E ; Berger, James M ; Nogales, Eva ; Botchan, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-8de97432e611f261034664caa205c764ad8b8b24c454a23193d60d94982dffa43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine triphosphatase</topic><topic>Adenosine Triphosphate - 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Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Clarey, Megan G</au><au>Erzberger, Jan P</au><au>Grob, Patricia</au><au>Leschziner, Andres E</au><au>Berger, James M</au><au>Nogales, Eva</au><au>Botchan, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2006-08-01</date><risdate>2006</risdate><volume>13</volume><issue>8</issue><spage>684</spage><epage>690</epage><pages>684-690</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the
Drosophila melanogaster
origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ domains in ORC contain a conserved structural element that, in DnaA, promotes formation of a right-handed helix, indicating that helical AAA+ substructures may be a feature of all initiators. A DnaA helical pentamer can be docked into ORC, and the location of Orc5 uniquely positions this core. The results suggest that ATP-dependent conformational changes observed in ORC derive from reorientation of the AAA+ domains. By analogy to the DNA-wrapping activity of DnaA, we posit that ORC together with Cdc6 prepares origin DNA for helicase loading through mechanisms related to the established pathway of prokaryotes.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>16829958</pmid><doi>10.1038/nsmb1121</doi><tpages>7</tpages></addata></record> |
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| subjects | Adenosine triphosphatase Adenosine Triphosphate - metabolism Amino Acid Sequence Animals ATP Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding proteins Biochemistry Biological Microscopy Biomedical and Life Sciences Cell Cycle Proteins - chemistry Cell Cycle Proteins - metabolism Deoxyribonucleic acid DNA DNA replication DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Drosophila melanogaster Drosophila Proteins - chemistry Drosophila Proteins - metabolism Life Sciences Membrane Biology Microscopy, Electron Models, Molecular Molecular biology Molecular Sequence Data Molecular structure Nucleotides Nucleotides - metabolism Origin Recognition Complex - chemistry Origin Recognition Complex - metabolism Physiological aspects Protein Conformation Protein Structure Proteins Sequence Homology, Amino Acid |
| title | Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex |
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