DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C-terminal region.
Identifieur interne : 002329 ( PubMed/Corpus ); précédent : 002328; suivant : 002330DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C-terminal region.
Auteurs : Noriko Shimazaki ; Takaya Yazaki ; Takashi Kubota ; Asami Sato ; Ayako Nakamura ; Shunsuke Kurei ; Shingo Toji ; Katsuyuki Tamai ; Osamu KoiwaiSource :
- Genes to cells : devoted to molecular & cellular mechanisms [ 1356-9597 ] ; 2005.
English descriptors
- KwdEn :
- Binding Sites, Cell Nucleus (metabolism), DNA Nucleotidylexotransferase (metabolism), DNA Polymerase beta (genetics), DNA Polymerase beta (metabolism), DNA Replication, Green Fluorescent Proteins (metabolism), Humans, Immunoprecipitation, In Vitro Techniques, Microscopy, Fluorescence, Mutagenesis, Site-Directed, Mutation, Proliferating Cell Nuclear Antigen (genetics), Proliferating Cell Nuclear Antigen (metabolism), Protein Binding, Protein Structure, Tertiary.
- MESH :
- chemical , genetics : DNA Polymerase beta, Proliferating Cell Nuclear Antigen.
- chemical , metabolism : DNA Nucleotidylexotransferase, DNA Polymerase beta, Green Fluorescent Proteins, Proliferating Cell Nuclear Antigen.
- metabolism : Cell Nucleus.
- Binding Sites, DNA Replication, Humans, Immunoprecipitation, In Vitro Techniques, Microscopy, Fluorescence, Mutagenesis, Site-Directed, Mutation, Protein Binding, Protein Structure, Tertiary.
Abstract
DNA polymerase lambda (Pol lambda) was recently identified as a new member of the family X of DNA polymerases. Here, we show that Pol lambda directly binds to proliferating cell nuclear antigen (PCNA), an auxiliary protein for DNA replication and repair enzymes, both in vitro and in vivo. A pull-down assay using deletion mutants of Pol lambda showed that the confined C-terminal region of Pol lambda directly binds to PCNA. Furthermore, a synthetic peptide of 20-mers derived from the C-terminal region of Pol lambda competes with full-length Pol lambda for binding to PCNA. The residues between amino acids 518 and 537 of Pol lambda are required for binding to PCNA, and are different from the consensus PCNA interacting motif (PIM). Pol lambda associates with PCNA in vivo by immunoprecipitation analysis and EGFP-tagged Pol lambda co-localizes with PCNA as spots within a nucleus using fluorescent microscopy. Through direct binding, PCNA suppressed the distributive nucleotidyltransferase activity of Pol lambda. Pol micro, which also belongs to the family X of DNA polymerases, binds to PCNA by a pivotal amino acid residue.
DOI: 10.1111/j.1365-2443.2005.00868.x
PubMed: 15966901
Links to Exploration step
pubmed:15966901Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C-terminal region.</title><author><name sortKey="Shimazaki, Noriko" sort="Shimazaki, Noriko" uniqKey="Shimazaki N" first="Noriko" last="Shimazaki">Noriko Shimazaki</name><affiliation><nlm:affiliation>Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan. snoriko@rs.noda.tus.ac.jp</nlm:affiliation></affiliation></author><author><name sortKey="Yazaki, Takaya" sort="Yazaki, Takaya" uniqKey="Yazaki T" first="Takaya" last="Yazaki">Takaya Yazaki</name></author><author><name sortKey="Kubota, Takashi" sort="Kubota, Takashi" uniqKey="Kubota T" first="Takashi" last="Kubota">Takashi Kubota</name></author><author><name sortKey="Sato, Asami" sort="Sato, Asami" uniqKey="Sato A" first="Asami" last="Sato">Asami Sato</name></author><author><name sortKey="Nakamura, Ayako" sort="Nakamura, Ayako" uniqKey="Nakamura A" first="Ayako" last="Nakamura">Ayako Nakamura</name></author><author><name sortKey="Kurei, Shunsuke" sort="Kurei, Shunsuke" uniqKey="Kurei S" first="Shunsuke" last="Kurei">Shunsuke Kurei</name></author><author><name sortKey="Toji, Shingo" sort="Toji, Shingo" uniqKey="Toji S" first="Shingo" last="Toji">Shingo Toji</name></author><author><name sortKey="Tamai, Katsuyuki" sort="Tamai, Katsuyuki" uniqKey="Tamai K" first="Katsuyuki" last="Tamai">Katsuyuki Tamai</name></author><author><name sortKey="Koiwai, Osamu" sort="Koiwai, Osamu" uniqKey="Koiwai O" first="Osamu" last="Koiwai">Osamu Koiwai</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15966901</idno><idno type="pmid">15966901</idno><idno type="doi">10.1111/j.1365-2443.2005.00868.x</idno><idno type="wicri:Area/PubMed/Corpus">002329</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002329</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C-terminal region.</title><author><name sortKey="Shimazaki, Noriko" sort="Shimazaki, Noriko" uniqKey="Shimazaki N" first="Noriko" last="Shimazaki">Noriko Shimazaki</name><affiliation><nlm:affiliation>Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan. snoriko@rs.noda.tus.ac.jp</nlm:affiliation></affiliation></author><author><name sortKey="Yazaki, Takaya" sort="Yazaki, Takaya" uniqKey="Yazaki T" first="Takaya" last="Yazaki">Takaya Yazaki</name></author><author><name sortKey="Kubota, Takashi" sort="Kubota, Takashi" uniqKey="Kubota T" first="Takashi" last="Kubota">Takashi Kubota</name></author><author><name sortKey="Sato, Asami" sort="Sato, Asami" uniqKey="Sato A" first="Asami" last="Sato">Asami Sato</name></author><author><name sortKey="Nakamura, Ayako" sort="Nakamura, Ayako" uniqKey="Nakamura A" first="Ayako" last="Nakamura">Ayako Nakamura</name></author><author><name sortKey="Kurei, Shunsuke" sort="Kurei, Shunsuke" uniqKey="Kurei S" first="Shunsuke" last="Kurei">Shunsuke Kurei</name></author><author><name sortKey="Toji, Shingo" sort="Toji, Shingo" uniqKey="Toji S" first="Shingo" last="Toji">Shingo Toji</name></author><author><name sortKey="Tamai, Katsuyuki" sort="Tamai, Katsuyuki" uniqKey="Tamai K" first="Katsuyuki" last="Tamai">Katsuyuki Tamai</name></author><author><name sortKey="Koiwai, Osamu" sort="Koiwai, Osamu" uniqKey="Koiwai O" first="Osamu" last="Koiwai">Osamu Koiwai</name></author></analytic><series><title level="j">Genes to cells : devoted to molecular & cellular mechanisms</title><idno type="ISSN">1356-9597</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cell Nucleus (metabolism)</term><term>DNA Nucleotidylexotransferase (metabolism)</term><term>DNA Polymerase beta (genetics)</term><term>DNA Polymerase beta (metabolism)</term><term>DNA Replication</term><term>Green Fluorescent Proteins (metabolism)</term><term>Humans</term><term>Immunoprecipitation</term><term>In Vitro Techniques</term><term>Microscopy, Fluorescence</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Proliferating Cell Nuclear Antigen (genetics)</term><term>Proliferating Cell Nuclear Antigen (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Polymerase beta</term><term>Proliferating Cell Nuclear Antigen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Nucleotidylexotransferase</term><term>DNA Polymerase beta</term><term>Green Fluorescent Proteins</term><term>Proliferating Cell Nuclear Antigen</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>DNA Replication</term><term>Humans</term><term>Immunoprecipitation</term><term>In Vitro Techniques</term><term>Microscopy, Fluorescence</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">DNA polymerase lambda (Pol lambda) was recently identified as a new member of the family X of DNA polymerases. Here, we show that Pol lambda directly binds to proliferating cell nuclear antigen (PCNA), an auxiliary protein for DNA replication and repair enzymes, both in vitro and in vivo. A pull-down assay using deletion mutants of Pol lambda showed that the confined C-terminal region of Pol lambda directly binds to PCNA. Furthermore, a synthetic peptide of 20-mers derived from the C-terminal region of Pol lambda competes with full-length Pol lambda for binding to PCNA. The residues between amino acids 518 and 537 of Pol lambda are required for binding to PCNA, and are different from the consensus PCNA interacting motif (PIM). Pol lambda associates with PCNA in vivo by immunoprecipitation analysis and EGFP-tagged Pol lambda co-localizes with PCNA as spots within a nucleus using fluorescent microscopy. Through direct binding, PCNA suppressed the distributive nucleotidyltransferase activity of Pol lambda. Pol micro, which also belongs to the family X of DNA polymerases, binds to PCNA by a pivotal amino acid residue.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15966901</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2014</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1356-9597</ISSN><JournalIssue CitedMedium="Print"><Volume>10</Volume><Issue>7</Issue><PubDate><Year>2005</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Genes to cells : devoted to molecular & cellular mechanisms</Title><ISOAbbreviation>Genes Cells</ISOAbbreviation></Journal><ArticleTitle>DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C-terminal region.</ArticleTitle><Pagination><MedlinePgn>705-15</MedlinePgn></Pagination><Abstract><AbstractText>DNA polymerase lambda (Pol lambda) was recently identified as a new member of the family X of DNA polymerases. Here, we show that Pol lambda directly binds to proliferating cell nuclear antigen (PCNA), an auxiliary protein for DNA replication and repair enzymes, both in vitro and in vivo. A pull-down assay using deletion mutants of Pol lambda showed that the confined C-terminal region of Pol lambda directly binds to PCNA. Furthermore, a synthetic peptide of 20-mers derived from the C-terminal region of Pol lambda competes with full-length Pol lambda for binding to PCNA. The residues between amino acids 518 and 537 of Pol lambda are required for binding to PCNA, and are different from the consensus PCNA interacting motif (PIM). Pol lambda associates with PCNA in vivo by immunoprecipitation analysis and EGFP-tagged Pol lambda co-localizes with PCNA as spots within a nucleus using fluorescent microscopy. Through direct binding, PCNA suppressed the distributive nucleotidyltransferase activity of Pol lambda. Pol micro, which also belongs to the family X of DNA polymerases, binds to PCNA by a pivotal amino acid residue.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shimazaki</LastName><ForeName>Noriko</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan. snoriko@rs.noda.tus.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yazaki</LastName><ForeName>Takaya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Kubota</LastName><ForeName>Takashi</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Asami</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Ayako</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kurei</LastName><ForeName>Shunsuke</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Toji</LastName><ForeName>Shingo</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Tamai</LastName><ForeName>Katsuyuki</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Koiwai</LastName><ForeName>Osamu</ForeName><Initials>O</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Genes Cells</MedlineTA><NlmUniqueID>9607379</NlmUniqueID><ISSNLinking>1356-9597</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018809">Proliferating Cell Nuclear Antigen</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C485184">enhanced green fluorescent protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.-</RegistryNumber><NameOfSubstance UI="D019951">DNA Polymerase beta</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.-</RegistryNumber><NameOfSubstance UI="C415367">DNA polymerase beta2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.31</RegistryNumber><NameOfSubstance UI="D004253">DNA Nucleotidylexotransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004253" MajorTopicYN="N">DNA Nucleotidylexotransferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019951" MajorTopicYN="N">DNA Polymerase beta</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004261" MajorTopicYN="N">DNA Replication</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018809" MajorTopicYN="N">Proliferating Cell Nuclear Antigen</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>6</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>9</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>6</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15966901</ArticleId><ArticleId IdType="pii">GTC868</ArticleId><ArticleId IdType="doi">10.1111/j.1365-2443.2005.00868.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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