Electron microscopic analysis reveals that replication factor C is sequestered by single-stranded DNA
Replication factor C (RF-C) is a eukaryotic hetero-pentameric protein required for DNA replication and repair processes by loading proliferating cell nuclear antigen (PCNA) onto DNA in an ATP-dependent manner. Prior to loading PCNA, RF-C binds to DNA. This binding is thought to be restricted to a sp...
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| Veröffentlicht in: | Nucleic acids research 1999-09, Vol.27 (17), p.3433-3437 |
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| container_title | Nucleic acids research |
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| creator | Keller, Robert C. Mossi, Romina Maga, Giovanni Wellinger, Ralf E. Hubscher, Ulrich Sogo, José M. |
| description | Replication factor C (RF-C) is a eukaryotic hetero-pentameric protein required for DNA replication and repair processes by loading proliferating cell nuclear antigen (PCNA) onto DNA in an ATP-dependent manner. Prior to loading PCNA, RF-C binds to DNA. This binding is thought to be restricted to a specific DNA structure, namely to a primer/template junction. Using the electron microscope we have examined the affinity of human heteropentameric RF-C and the DNA-binding region within the large subunit of RF-C from Drosophila melanogaster (dRF-Cp140) to heteroduplex DNA. The electron microscopic data indicate that both human heteropentameric RF-C and the DNA-binding region within dRF-Cp140 are sequestered by single-stranded DNA. No preferential affinity for the 3′ or 5′ transition points from single- to double-stranded DNA was evident. |
| doi_str_mv | 10.1093/nar/27.17.3433 |
| format | Article |
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Prior to loading PCNA, RF-C binds to DNA. This binding is thought to be restricted to a specific DNA structure, namely to a primer/template junction. Using the electron microscope we have examined the affinity of human heteropentameric RF-C and the DNA-binding region within the large subunit of RF-C from Drosophila melanogaster (dRF-Cp140) to heteroduplex DNA. The electron microscopic data indicate that both human heteropentameric RF-C and the DNA-binding region within dRF-Cp140 are sequestered by single-stranded DNA. No preferential affinity for the 3′ or 5′ transition points from single- to double-stranded DNA was evident.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/27.17.3433</identifier><identifier>PMID: 10446230</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; DNA, Single-Stranded - chemistry ; DNA, Single-Stranded - physiology ; DNA, Single-Stranded - ultrastructure ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - physiology ; DNA-Binding Proteins - ultrastructure ; Drosophila - chemistry ; Drosophila melanogaster ; HeLa Cells ; Homeodomain Proteins ; Humans ; Microscopy, Electron ; Minor Histocompatibility Antigens ; Nucleic Acid Heteroduplexes - ultrastructure ; Plasmids - chemistry ; Protein Binding ; Proto-Oncogene Proteins c-bcl-2 ; Replication Protein C ; Repressor Proteins ; Saccharomyces cerevisiae Proteins</subject><ispartof>Nucleic acids research, 1999-09, Vol.27 (17), p.3433-3437</ispartof><rights>Copyright Oxford University Press(England) Sep 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481t-51418d89d7552a8f549c10e749b7fdeab0dd5d01bef9a055761658c05e1e42633</citedby><cites>FETCH-LOGICAL-c481t-51418d89d7552a8f549c10e749b7fdeab0dd5d01bef9a055761658c05e1e42633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC148584/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC148584/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10446230$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Keller, Robert C.</creatorcontrib><creatorcontrib>Mossi, Romina</creatorcontrib><creatorcontrib>Maga, Giovanni</creatorcontrib><creatorcontrib>Wellinger, Ralf E.</creatorcontrib><creatorcontrib>Hubscher, Ulrich</creatorcontrib><creatorcontrib>Sogo, José M.</creatorcontrib><title>Electron microscopic analysis reveals that replication factor C is sequestered by single-stranded DNA</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Research</addtitle><description>Replication factor C (RF-C) is a eukaryotic hetero-pentameric protein required for DNA replication and repair processes by loading proliferating cell nuclear antigen (PCNA) onto DNA in an ATP-dependent manner. 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No preferential affinity for the 3′ or 5′ transition points from single- to double-stranded DNA was evident.</description><subject>Animals</subject><subject>DNA, Single-Stranded - chemistry</subject><subject>DNA, Single-Stranded - physiology</subject><subject>DNA, Single-Stranded - ultrastructure</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - physiology</subject><subject>DNA-Binding Proteins - ultrastructure</subject><subject>Drosophila - chemistry</subject><subject>Drosophila melanogaster</subject><subject>HeLa Cells</subject><subject>Homeodomain Proteins</subject><subject>Humans</subject><subject>Microscopy, Electron</subject><subject>Minor Histocompatibility Antigens</subject><subject>Nucleic Acid Heteroduplexes - ultrastructure</subject><subject>Plasmids - chemistry</subject><subject>Protein Binding</subject><subject>Proto-Oncogene Proteins c-bcl-2</subject><subject>Replication Protein C</subject><subject>Repressor Proteins</subject><subject>Saccharomyces cerevisiae Proteins</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1P3DAQxS3UCraUK8cq4sAtix1_JQcOdKFQCYGqUglxsRx7AqbZeGtnUfe_72wXIcqlJ8szv3l6M4-QfUanjDb8aLDpqNJTpqdccL5FJoyrqhSNqt6RCeVUloyKeod8yPmRUiaYFNtkB2tCVZxOCJz14MYUh2IeXIrZxUVwhR1sv8ohFwmewPa5GB_siJ9FH5wdA9KddWNMxaxAKMOvJeQREviiXRU5DPc9lHlMdvBYOr06-UjedygDe8_vLvnx5exmdlFeXp9_nZ1clk7UbCwl-qt93XgtZWXrTorGMQpaNK3uPNiWei89ZS10jaVSasWUrB2VwEBUivNdcrzRXSzbOXgHA5rozSKFuU0rE20w_3aG8GDu45Nhopa1wPnD5_kU_-5k5iE76Hs7QFxmoxo8rODqvyDTXEjO1ooHb8DHuEx43mwqiisgpRGabqB1AjlB9-KYUbOO2WDMptIoa9Yx48Cn13u-wje5IlBugIC5_H7p2_TTKM21NBe3d0Z_Pv9-w74pc8X_AOkptAY</recordid><startdate>199909</startdate><enddate>199909</enddate><creator>Keller, Robert C.</creator><creator>Mossi, Romina</creator><creator>Maga, Giovanni</creator><creator>Wellinger, Ralf E.</creator><creator>Hubscher, Ulrich</creator><creator>Sogo, José M.</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199909</creationdate><title>Electron microscopic analysis reveals that replication factor C is sequestered by single-stranded DNA</title><author>Keller, Robert C. ; 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| source | OUP_牛津大学出版社OA刊; MEDLINE; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals DNA, Single-Stranded - chemistry DNA, Single-Stranded - physiology DNA, Single-Stranded - ultrastructure DNA-Binding Proteins - chemistry DNA-Binding Proteins - physiology DNA-Binding Proteins - ultrastructure Drosophila - chemistry Drosophila melanogaster HeLa Cells Homeodomain Proteins Humans Microscopy, Electron Minor Histocompatibility Antigens Nucleic Acid Heteroduplexes - ultrastructure Plasmids - chemistry Protein Binding Proto-Oncogene Proteins c-bcl-2 Replication Protein C Repressor Proteins Saccharomyces cerevisiae Proteins |
| title | Electron microscopic analysis reveals that replication factor C is sequestered by single-stranded DNA |
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