Two novel human and mouse DNA polymerases of the polX family
We describe here two novel mouse and human DNA polymerases: one (pol lambda) has homology with DNA polymerase beta while the other one (pol mu) is closer to terminal deoxynucleotidyltransferase. However both have DNA polymerase activity in vitro and share similar structural organization, including a...
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Veröffentlicht in: | Nucleic acids research 2000-09, Vol.28 (18), p.3684-3693 |
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creator | Aoufouchi, S Flatter, E Dahan, A Faili, A Bertocci, B Storck, S Delbos, F Cocea, L Gupta, N Weill, J C Reynaud, C A |
description | We describe here two novel mouse and human DNA polymerases: one (pol lambda) has homology with DNA polymerase beta while the other one (pol mu) is closer to terminal deoxynucleotidyltransferase. However both have DNA polymerase activity in vitro and share similar structural organization, including a BRCT domain, helix-loop-helix DNA-binding motifs and polymerase X domain. mRNA expression of pol lambda is highest in testis and fetal liver, while expression of pol mu is more lymphoid, with highest expression both in thymus and tonsillar B cells. An unusually large number of splice variants is observed for the pol mu gene, most of which affect the polymerase domain. Expression of mRNA of both polymerases is down-regulated upon treatment by DNA damaging agents (UV light, gamma-rays or H(2)O(2)). This suggests that their biological function may differ from DNA translesion synthesis, for which several DNA polymerase activities have been recently described. Possible functions are discussed. |
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However both have DNA polymerase activity in vitro and share similar structural organization, including a BRCT domain, helix-loop-helix DNA-binding motifs and polymerase X domain. mRNA expression of pol lambda is highest in testis and fetal liver, while expression of pol mu is more lymphoid, with highest expression both in thymus and tonsillar B cells. An unusually large number of splice variants is observed for the pol mu gene, most of which affect the polymerase domain. Expression of mRNA of both polymerases is down-regulated upon treatment by DNA damaging agents (UV light, gamma-rays or H(2)O(2)). This suggests that their biological function may differ from DNA translesion synthesis, for which several DNA polymerase activities have been recently described. Possible functions are discussed.</description><identifier>ISSN: 1362-4962</identifier><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/28.18.3684</identifier><identifier>PMID: 10982892</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>England: Oxford Publishing Limited (England)</publisher><subject>Alternative Splicing ; Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA Damage ; DNA Polymerase beta - chemistry ; DNA Polymerase beta - classification ; DNA, Complementary - isolation & purification ; DNA-Directed DNA Polymerase - chemistry ; DNA-Directed DNA Polymerase - classification ; DNA-Directed DNA Polymerase - isolation & purification ; Escherichia coli ; Gene Expression Regulation, Enzymologic ; Humans ; Mice ; Molecular Sequence Data ; Phylogeny ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Tissue Distribution ; Tumor Cells, Cultured</subject><ispartof>Nucleic acids research, 2000-09, Vol.28 (18), p.3684-3693</ispartof><rights>Copyright Oxford University Press(England) Sep 15, 2000</rights><rights>Copyright © 2000 Oxford University Press 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-aed03e18ec759665fd2866f8588ee9991059a242d5bed38167442656cfeb2b6d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC110747/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC110747/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10982892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aoufouchi, S</creatorcontrib><creatorcontrib>Flatter, E</creatorcontrib><creatorcontrib>Dahan, A</creatorcontrib><creatorcontrib>Faili, A</creatorcontrib><creatorcontrib>Bertocci, B</creatorcontrib><creatorcontrib>Storck, S</creatorcontrib><creatorcontrib>Delbos, F</creatorcontrib><creatorcontrib>Cocea, L</creatorcontrib><creatorcontrib>Gupta, N</creatorcontrib><creatorcontrib>Weill, J C</creatorcontrib><creatorcontrib>Reynaud, C A</creatorcontrib><title>Two novel human and mouse DNA polymerases of the polX family</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>We describe here two novel mouse and human DNA polymerases: one (pol lambda) has homology with DNA polymerase beta while the other one (pol mu) is closer to terminal deoxynucleotidyltransferase. However both have DNA polymerase activity in vitro and share similar structural organization, including a BRCT domain, helix-loop-helix DNA-binding motifs and polymerase X domain. mRNA expression of pol lambda is highest in testis and fetal liver, while expression of pol mu is more lymphoid, with highest expression both in thymus and tonsillar B cells. An unusually large number of splice variants is observed for the pol mu gene, most of which affect the polymerase domain. Expression of mRNA of both polymerases is down-regulated upon treatment by DNA damaging agents (UV light, gamma-rays or H(2)O(2)). This suggests that their biological function may differ from DNA translesion synthesis, for which several DNA polymerase activities have been recently described. Possible functions are discussed.</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>DNA Damage</subject><subject>DNA Polymerase beta - chemistry</subject><subject>DNA Polymerase beta - classification</subject><subject>DNA, Complementary - isolation & purification</subject><subject>DNA-Directed DNA Polymerase - chemistry</subject><subject>DNA-Directed DNA Polymerase - classification</subject><subject>DNA-Directed DNA Polymerase - isolation & purification</subject><subject>Escherichia coli</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tissue Distribution</subject><subject>Tumor Cells, Cultured</subject><issn>1362-4962</issn><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUU1Lw0AUXESxtXr1KIsHb233OxvQQ6mfUPRSwduySV5sSpKtu02l_96EFqme3uO9mWGGQeiSkhElMR_X1o-ZHlE94kqLI9SnXLGhiBU7Pth76CyEJSFUUClOUa-laqZj1ke382-Ha7eBEi-aytbY1hmuXBMA379O8MqV2wq8DRCwy_F6Ad3pA-e2KsrtOTrJbRngYj8H6P3xYT59Hs7enl6mk9kwFYKuhxYywoFqSCMZKyXzjGmlci21BojjmBIZWyZYJhPIuKYqEoIpqdIcEpaojA_Q3U531SQVZCnUa29Ls_JFZf3WOFuYv5-6WJhPtzGUkkhELf9mz_fuq4GwNlURUihLW0Mb1dBIMc4paYHX_4BL1_i6zWYYIVJJpjq10Q6UeheCh_zXCCWmK8W0pRimDdWmK6UlXB3aP4DvWuA_70CHmw</recordid><startdate>20000915</startdate><enddate>20000915</enddate><creator>Aoufouchi, S</creator><creator>Flatter, E</creator><creator>Dahan, A</creator><creator>Faili, A</creator><creator>Bertocci, B</creator><creator>Storck, S</creator><creator>Delbos, F</creator><creator>Cocea, L</creator><creator>Gupta, N</creator><creator>Weill, J C</creator><creator>Reynaud, C A</creator><general>Oxford Publishing Limited (England)</general><general>Oxford University Press</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>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>5PM</scope></search><sort><creationdate>20000915</creationdate><title>Two novel human and mouse DNA polymerases of the polX family</title><author>Aoufouchi, S ; 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However both have DNA polymerase activity in vitro and share similar structural organization, including a BRCT domain, helix-loop-helix DNA-binding motifs and polymerase X domain. mRNA expression of pol lambda is highest in testis and fetal liver, while expression of pol mu is more lymphoid, with highest expression both in thymus and tonsillar B cells. An unusually large number of splice variants is observed for the pol mu gene, most of which affect the polymerase domain. Expression of mRNA of both polymerases is down-regulated upon treatment by DNA damaging agents (UV light, gamma-rays or H(2)O(2)). This suggests that their biological function may differ from DNA translesion synthesis, for which several DNA polymerase activities have been recently described. Possible functions are discussed.</abstract><cop>England</cop><pub>Oxford Publishing Limited (England)</pub><pmid>10982892</pmid><doi>10.1093/nar/28.18.3684</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Alternative Splicing Amino Acid Sequence Animals Cell Line Cloning, Molecular DNA Damage DNA Polymerase beta - chemistry DNA Polymerase beta - classification DNA, Complementary - isolation & purification DNA-Directed DNA Polymerase - chemistry DNA-Directed DNA Polymerase - classification DNA-Directed DNA Polymerase - isolation & purification Escherichia coli Gene Expression Regulation, Enzymologic Humans Mice Molecular Sequence Data Phylogeny Protein Conformation Protein Structure, Tertiary Sequence Homology, Amino Acid Tissue Distribution Tumor Cells, Cultured |
title | Two novel human and mouse DNA polymerases of the polX family |
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