A specific 3′ exonuclease activity of UvrABC
Specific cutting of undamaged DNA by UvrABC nuclease is observed. It occurs seven nucleotides (nt) from the 3′ terminus of oligonucleotides annealed to single‐stranded M13 DNA circles. Although the location of the UvrABC cut on undamaged DNA is similar to that of the cut on the 5′ side of a damaged...
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description | Specific cutting of undamaged DNA by UvrABC nuclease is observed. It occurs seven nucleotides (nt) from the 3′ terminus of oligonucleotides annealed to single‐stranded M13 DNA circles. Although the location of the UvrABC cut on undamaged DNA is similar to that of the cut on the 5′ side of a damaged DNA site during the dual incision reaction, the cut of undamaged DNA is not an intermediate in the dual incision step. On DNA duplexes with a single AAF adduct, the anticipated cut at the eighth phosphodiester bond 5′ of the lesion is present, but extra cuts at 7‐nt increments are observed at the 15th and 22nd phosphodiester bonds. We suggest that these additional cuts are made by the UvrABC activity observed on undamaged DNA; such activity is referred to as ABC 3′ exonuclease and may play a significant role by providing a suitable gap for RecA‐mediated recombinational exchanges during repair of interstrand crosslinks and closely opposed lesions. This ABC 3′ exonuclease activity depends on higher concentrations of Uvr proteins as compared with dual incision and may be relevant to reactions that occur when UvrA and UvrB are increased during SOS induction. |
doi_str_mv | 10.1093/emboj/17.2.626 |
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It occurs seven nucleotides (nt) from the 3′ terminus of oligonucleotides annealed to single‐stranded M13 DNA circles. Although the location of the UvrABC cut on undamaged DNA is similar to that of the cut on the 5′ side of a damaged DNA site during the dual incision reaction, the cut of undamaged DNA is not an intermediate in the dual incision step. On DNA duplexes with a single AAF adduct, the anticipated cut at the eighth phosphodiester bond 5′ of the lesion is present, but extra cuts at 7‐nt increments are observed at the 15th and 22nd phosphodiester bonds. We suggest that these additional cuts are made by the UvrABC activity observed on undamaged DNA; such activity is referred to as ABC 3′ exonuclease and may play a significant role by providing a suitable gap for RecA‐mediated recombinational exchanges during repair of interstrand crosslinks and closely opposed lesions. 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It occurs seven nucleotides (nt) from the 3′ terminus of oligonucleotides annealed to single‐stranded M13 DNA circles. Although the location of the UvrABC cut on undamaged DNA is similar to that of the cut on the 5′ side of a damaged DNA site during the dual incision reaction, the cut of undamaged DNA is not an intermediate in the dual incision step. On DNA duplexes with a single AAF adduct, the anticipated cut at the eighth phosphodiester bond 5′ of the lesion is present, but extra cuts at 7‐nt increments are observed at the 15th and 22nd phosphodiester bonds. We suggest that these additional cuts are made by the UvrABC activity observed on undamaged DNA; such activity is referred to as ABC 3′ exonuclease and may play a significant role by providing a suitable gap for RecA‐mediated recombinational exchanges during repair of interstrand crosslinks and closely opposed lesions. This ABC 3′ exonuclease activity depends on higher concentrations of Uvr proteins as compared with dual incision and may be relevant to reactions that occur when UvrA and UvrB are increased during SOS induction.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>DNA Damage</subject><subject>DNA Helicases</subject><subject>DNA Repair</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Endodeoxyribonucleases</subject><subject>Enzyme Activation - genetics</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins</subject><subject>Exonucleases - metabolism</subject><subject>RecA-mediated exchanges</subject><subject>SOS response</subject><subject>UvrABC 3′ exonuclease</subject><subject>UvrABC 5′ side cut</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1uEzEUhS0EKqGwZYc0K3Yz8R2P_zZIaVTKTyksWlhajnOnOEzGqT0Tmh3PxCPxJEyZKIIF6urKOuc7vvYh5DnQAqhmU1wvwmoKsigLUYoHZAKVoHlJJX9IJrQUkFeg9GPyJKUVpZQrCUfkSFeMCs4mpJhlaYPO195l7NePnxnehrZ3DdqEmXWd3_pul4U6u9rG2cn8KXlU2ybhs_08JlevTy_nb_Lzj2dv57Pz3PGq1Lm2rGRYuWHaSrKqBusUV0gXS2Y510opzi1oK2uFWFtUdjmcBDBW1xyX7Ji8GnM3_WKNS4dtF21jNtGvbdyZYL35V2n9V3MdtgZA0grKIeDlPiCGmx5TZ9Y-OWwa22Lok5FacCmUuNcIgoEGepdYjEYXQ0oR68M2QM1dFeZPFQakKc1QxQC8-PsNB_v-7wddjvp33-DunjRz-uHkneSaSqkHcjqSaYDaa4xmFfrYDoX8f5d8JHzq8PZwl43fjJBMcvPl4sxcis8XEt5X5hP7DQj2tlI</recordid><startdate>19980115</startdate><enddate>19980115</enddate><creator>Gordienko, Irina</creator><creator>Rupp, W.Dean</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</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>7TM</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980115</creationdate><title>A specific 3′ exonuclease activity of UvrABC</title><author>Gordienko, Irina ; Rupp, W.Dean</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5429-9a323e4c9a3a4734f1ac858e0bd3a55988855a19a7f8eefae8ad19a6133ff5ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>DNA Damage</topic><topic>DNA Helicases</topic><topic>DNA Repair</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Endodeoxyribonucleases</topic><topic>Enzyme Activation - genetics</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins</topic><topic>Exonucleases - metabolism</topic><topic>RecA-mediated exchanges</topic><topic>SOS response</topic><topic>UvrABC 3′ exonuclease</topic><topic>UvrABC 5′ side cut</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gordienko, Irina</creatorcontrib><creatorcontrib>Rupp, W.Dean</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gordienko, Irina</au><au>Rupp, W.Dean</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A specific 3′ exonuclease activity of UvrABC</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>1998-01-15</date><risdate>1998</risdate><volume>17</volume><issue>2</issue><spage>626</spage><epage>633</epage><pages>626-633</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><abstract>Specific cutting of undamaged DNA by UvrABC nuclease is observed. It occurs seven nucleotides (nt) from the 3′ terminus of oligonucleotides annealed to single‐stranded M13 DNA circles. Although the location of the UvrABC cut on undamaged DNA is similar to that of the cut on the 5′ side of a damaged DNA site during the dual incision reaction, the cut of undamaged DNA is not an intermediate in the dual incision step. On DNA duplexes with a single AAF adduct, the anticipated cut at the eighth phosphodiester bond 5′ of the lesion is present, but extra cuts at 7‐nt increments are observed at the 15th and 22nd phosphodiester bonds. We suggest that these additional cuts are made by the UvrABC activity observed on undamaged DNA; such activity is referred to as ABC 3′ exonuclease and may play a significant role by providing a suitable gap for RecA‐mediated recombinational exchanges during repair of interstrand crosslinks and closely opposed lesions. This ABC 3′ exonuclease activity depends on higher concentrations of Uvr proteins as compared with dual incision and may be relevant to reactions that occur when UvrA and UvrB are increased during SOS induction.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>9430653</pmid><doi>10.1093/emboj/17.2.626</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism DNA Damage DNA Helicases DNA Repair DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Endodeoxyribonucleases Enzyme Activation - genetics Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins Exonucleases - metabolism RecA-mediated exchanges SOS response UvrABC 3′ exonuclease UvrABC 5′ side cut |
title | A specific 3′ exonuclease activity of UvrABC |
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