Loading…

ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA

Two nucleases that catalyze the excision of photoproducts from UV-irradiated DNA have been extensively purified from M. luteus ( M. lysodeikticus ). The first enzyme, an endonuclease, has been purified 5000-fold and is free of conflicting nuclease activities. It introduces single-strand breaks into...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1969-05, Vol.63 (1), p.144-151
Main Authors: Kaplan, Joan C., Kushner, Sidney R., Grossman, Lawrence
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c2264-265c2079955fd72dca0525a71dfb39816fa9b25f57c14e379528c770570e60ba3
cites
container_end_page 151
container_issue 1
container_start_page 144
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 63
creator Kaplan, Joan C.
Kushner, Sidney R.
Grossman, Lawrence
description Two nucleases that catalyze the excision of photoproducts from UV-irradiated DNA have been extensively purified from M. luteus ( M. lysodeikticus ). The first enzyme, an endonuclease, has been purified 5000-fold and is free of conflicting nuclease activities. It introduces single-strand breaks into irradiated DNA but does not act on native or single-stranded DNA. The purified enzyme is activated but not dependent on Mg ++ and has an approximate molecular weight of 15,000. Photoproduct excision is absolutely dependent on the second enzyme, a magnesium requiring exonuclease. This enzyme, which has been purified 1000-fold, is devoid of conflicting nucleases. It hydrolyzes irradiated and unirradiated denatured DNA at the same rate, but has no activity on RNA. It only acts on double-stranded DNA which has been both irradiated and pretreated with the endonuclease. The combined action of the endo- and exonuclease results in the quantitative removal of photoproduct regions from UV-irradiated DNA. Approximately five nucleotides are released for every single-strand incision.
doi_str_mv 10.1073/pnas.63.1.144
format article
fullrecord <record><control><sourceid>pnas_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1073_pnas_63_1_144</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>63_1_144</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2264-265c2079955fd72dca0525a71dfb39816fa9b25f57c14e379528c770570e60ba3</originalsourceid><addsrcrecordid>eNp9UUtP4zAQthAIuoUjNw6-cNuEsWPH9YFD1LrUUpqgNC2Pi-WmyW5RX0patHvdX74uL8GF04y-x3wafQidE_AJiOBqs7KNHwY-8QljB6hFQBIvZBIOUQuACq_DKDtBP5rmCQAk78AxOuaUCxlCC_1TyePDMMp1F2fqNtIZTvu4l0Q_sfbx7TjTfd11bJrs8fwuxS96NcI6maTxRPXcgvOBwuq-q0fvusHDUCcK9_RQZSPcz9IhHsd5Fk10Gqvc01kW9XSUO7eLOkVHlV005dnbbKNxX-XdgRenNy489gpKQ-bRkBcUhJScVzNBZ4UF94UVZFZNA9khYWXllPKKi4KwMhCS004hBHABZQhTG7TR9evdzW66LGdFudrWdmE29Xxp679mbefmK7Oa_za_1s-GBwwIc37v1V_U66apy-rDSsDsqzD7KkwYGGJcFU5_8Za3h9-1n-jLb2hT7RaLbflnG_wHOBGIIw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA</title><source>JSTOR Archival Journals and Primary Sources Collection</source><source>PubMed Central</source><creator>Kaplan, Joan C. ; Kushner, Sidney R. ; Grossman, Lawrence</creator><creatorcontrib>Kaplan, Joan C. ; Kushner, Sidney R. ; Grossman, Lawrence</creatorcontrib><description>Two nucleases that catalyze the excision of photoproducts from UV-irradiated DNA have been extensively purified from M. luteus ( M. lysodeikticus ). The first enzyme, an endonuclease, has been purified 5000-fold and is free of conflicting nuclease activities. It introduces single-strand breaks into irradiated DNA but does not act on native or single-stranded DNA. The purified enzyme is activated but not dependent on Mg ++ and has an approximate molecular weight of 15,000. Photoproduct excision is absolutely dependent on the second enzyme, a magnesium requiring exonuclease. This enzyme, which has been purified 1000-fold, is devoid of conflicting nucleases. It hydrolyzes irradiated and unirradiated denatured DNA at the same rate, but has no activity on RNA. It only acts on double-stranded DNA which has been both irradiated and pretreated with the endonuclease. The combined action of the endo- and exonuclease results in the quantitative removal of photoproduct regions from UV-irradiated DNA. Approximately five nucleotides are released for every single-strand incision.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.63.1.144</identifier><identifier>PMID: 5257960</identifier><language>eng</language><publisher>National Acad Sciences</publisher><subject>Biological Sciences: Biochemistry</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1969-05, Vol.63 (1), p.144-151</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2264-265c2079955fd72dca0525a71dfb39816fa9b25f57c14e379528c770570e60ba3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/63/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC534014/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC534014/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids></links><search><creatorcontrib>Kaplan, Joan C.</creatorcontrib><creatorcontrib>Kushner, Sidney R.</creatorcontrib><creatorcontrib>Grossman, Lawrence</creatorcontrib><title>ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA</title><title>Proceedings of the National Academy of Sciences - PNAS</title><description>Two nucleases that catalyze the excision of photoproducts from UV-irradiated DNA have been extensively purified from M. luteus ( M. lysodeikticus ). The first enzyme, an endonuclease, has been purified 5000-fold and is free of conflicting nuclease activities. It introduces single-strand breaks into irradiated DNA but does not act on native or single-stranded DNA. The purified enzyme is activated but not dependent on Mg ++ and has an approximate molecular weight of 15,000. Photoproduct excision is absolutely dependent on the second enzyme, a magnesium requiring exonuclease. This enzyme, which has been purified 1000-fold, is devoid of conflicting nucleases. It hydrolyzes irradiated and unirradiated denatured DNA at the same rate, but has no activity on RNA. It only acts on double-stranded DNA which has been both irradiated and pretreated with the endonuclease. The combined action of the endo- and exonuclease results in the quantitative removal of photoproduct regions from UV-irradiated DNA. Approximately five nucleotides are released for every single-strand incision.</description><subject>Biological Sciences: Biochemistry</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><recordid>eNp9UUtP4zAQthAIuoUjNw6-cNuEsWPH9YFD1LrUUpqgNC2Pi-WmyW5RX0patHvdX74uL8GF04y-x3wafQidE_AJiOBqs7KNHwY-8QljB6hFQBIvZBIOUQuACq_DKDtBP5rmCQAk78AxOuaUCxlCC_1TyePDMMp1F2fqNtIZTvu4l0Q_sfbx7TjTfd11bJrs8fwuxS96NcI6maTxRPXcgvOBwuq-q0fvusHDUCcK9_RQZSPcz9IhHsd5Fk10Gqvc01kW9XSUO7eLOkVHlV005dnbbKNxX-XdgRenNy489gpKQ-bRkBcUhJScVzNBZ4UF94UVZFZNA9khYWXllPKKi4KwMhCS004hBHABZQhTG7TR9evdzW66LGdFudrWdmE29Xxp679mbefmK7Oa_za_1s-GBwwIc37v1V_U66apy-rDSsDsqzD7KkwYGGJcFU5_8Za3h9-1n-jLb2hT7RaLbflnG_wHOBGIIw</recordid><startdate>19690501</startdate><enddate>19690501</enddate><creator>Kaplan, Joan C.</creator><creator>Kushner, Sidney R.</creator><creator>Grossman, Lawrence</creator><general>National Acad Sciences</general><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>19690501</creationdate><title>ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA</title><author>Kaplan, Joan C. ; Kushner, Sidney R. ; Grossman, Lawrence</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2264-265c2079955fd72dca0525a71dfb39816fa9b25f57c14e379528c770570e60ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Biological Sciences: Biochemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kaplan, Joan C.</creatorcontrib><creatorcontrib>Kushner, Sidney R.</creatorcontrib><creatorcontrib>Grossman, Lawrence</creatorcontrib><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaplan, Joan C.</au><au>Kushner, Sidney R.</au><au>Grossman, Lawrence</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1969-05-01</date><risdate>1969</risdate><volume>63</volume><issue>1</issue><spage>144</spage><epage>151</epage><pages>144-151</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Two nucleases that catalyze the excision of photoproducts from UV-irradiated DNA have been extensively purified from M. luteus ( M. lysodeikticus ). The first enzyme, an endonuclease, has been purified 5000-fold and is free of conflicting nuclease activities. It introduces single-strand breaks into irradiated DNA but does not act on native or single-stranded DNA. The purified enzyme is activated but not dependent on Mg ++ and has an approximate molecular weight of 15,000. Photoproduct excision is absolutely dependent on the second enzyme, a magnesium requiring exonuclease. This enzyme, which has been purified 1000-fold, is devoid of conflicting nucleases. It hydrolyzes irradiated and unirradiated denatured DNA at the same rate, but has no activity on RNA. It only acts on double-stranded DNA which has been both irradiated and pretreated with the endonuclease. The combined action of the endo- and exonuclease results in the quantitative removal of photoproduct regions from UV-irradiated DNA. Approximately five nucleotides are released for every single-strand incision.</abstract><pub>National Acad Sciences</pub><pmid>5257960</pmid><doi>10.1073/pnas.63.1.144</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 1969-05, Vol.63 (1), p.144-151
issn 0027-8424
1091-6490
language eng
recordid cdi_crossref_primary_10_1073_pnas_63_1_144
source JSTOR Archival Journals and Primary Sources Collection; PubMed Central
subjects Biological Sciences: Biochemistry
title ENZYMATIC REPAIR OF DNA, I. PURIFICATION OF TWO ENZYMES INVOLVED IN THE EXCISION OF THYMINE DIMERS FROM ULTRAVIOLET-IRRADIATED DNA
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T10%3A32%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pnas_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=ENZYMATIC%20REPAIR%20OF%20DNA,%20I.%20PURIFICATION%20OF%20TWO%20ENZYMES%20INVOLVED%20IN%20THE%20EXCISION%20OF%20THYMINE%20DIMERS%20FROM%20ULTRAVIOLET-IRRADIATED%20DNA&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Kaplan,%20Joan%20C.&rft.date=1969-05-01&rft.volume=63&rft.issue=1&rft.spage=144&rft.epage=151&rft.pages=144-151&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.63.1.144&rft_dat=%3Cpnas_cross%3E63_1_144%3C/pnas_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c2264-265c2079955fd72dca0525a71dfb39816fa9b25f57c14e379528c770570e60ba3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/5257960&rfr_iscdi=true