Characterization in vitro and in vivo of the DNA helicase encoded by Deinococcus radiodurans locus DR1572
Deinococcus radiodurans survives extremely high doses of ionizing and ultraviolet radiation and treatment with various DNA-damaging chemicals. As an effort to identify and characterize proteins that function in DNA repair in this organism, we have studied the protein encoded by locus DR1572. This ge...
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| Veröffentlicht in: | DNA repair 2009-05, Vol.8 (5), p.612-619 |
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| description | Deinococcus radiodurans survives extremely high doses of ionizing and ultraviolet radiation and treatment with various DNA-damaging chemicals. As an effort to identify and characterize proteins that function in DNA repair in this organism, we have studied the protein encoded by locus DR1572. This gene is predicted to encode a Superfamily I DNA helicase, except that genome sequencing indicated that it has a one-base frameshift and would not encode a complete helicase. We have cloned the gene from two different
D. radiodurans strains and find that the frameshift mutation is not present. The corrected gene encodes a 755 residue protein that is similar to the
Bacillus subtilis YvgS protein and to helicase IV of
Escherichia coli. The purified protein (helicase IV
Dr) has ATP hydrolysis and DNA helicase activity. A truncated protein that lacks 214 residues from the N-terminus, which precede the conserved helicase domain, has greater ATPase activity than the full-length protein but has no detectable helicase activity. Disruption of locus DR1572 in the
D. radiodurans chromosome causes greater sensitivity to hydrogen peroxide and methyl-methanesulfonate compared to wild-type cells, but no change in resistance to gamma and ultraviolet radiation and to mitomycin C. The results indicate that locus DR1572 encodes a complete protein that contributes to DNA metabolism in
D. radiodurans. |
| doi_str_mv | 10.1016/j.dnarep.2008.12.011 |
| format | Article |
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D. radiodurans strains and find that the frameshift mutation is not present. The corrected gene encodes a 755 residue protein that is similar to the
Bacillus subtilis YvgS protein and to helicase IV of
Escherichia coli. The purified protein (helicase IV
Dr) has ATP hydrolysis and DNA helicase activity. A truncated protein that lacks 214 residues from the N-terminus, which precede the conserved helicase domain, has greater ATPase activity than the full-length protein but has no detectable helicase activity. Disruption of locus DR1572 in the
D. radiodurans chromosome causes greater sensitivity to hydrogen peroxide and methyl-methanesulfonate compared to wild-type cells, but no change in resistance to gamma and ultraviolet radiation and to mitomycin C. The results indicate that locus DR1572 encodes a complete protein that contributes to DNA metabolism in
D. radiodurans.</description><identifier>ISSN: 1568-7864</identifier><identifier>EISSN: 1568-7856</identifier><identifier>DOI: 10.1016/j.dnarep.2008.12.011</identifier><identifier>PMID: 19179120</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Antineoplastic Agents, Alkylating - pharmacology ; Bacillus subtilis ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Blotting, Southern ; Cloning, Molecular ; Deinococcus - enzymology ; Deinococcus - genetics ; Deinococcus radiodurans ; DNA damage ; DNA Damage - drug effects ; DNA Damage - radiation effects ; DNA Helicases - genetics ; DNA Helicases - metabolism ; DNA repair ; DNA Repair - drug effects ; DNA Repair - radiation effects ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Gamma Rays ; Growth, nutrition, cell differenciation ; Helicase IV ; Hydrogen Peroxide - pharmacology ; Hydrolysis - drug effects ; Hydrolysis - radiation effects ; In Vitro Techniques ; Methyl Methanesulfonate - pharmacology ; Microbiology ; Mitomycin - pharmacology ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Mutagenesis. Repair ; Mutation - genetics ; Nucleic Acid Synthesis Inhibitors - pharmacology ; Oxidants - pharmacology ; Polymerase Chain Reaction ; RecF pathway ; Sequence Homology, Amino Acid ; Ultraviolet Rays</subject><ispartof>DNA repair, 2009-05, Vol.8 (5), p.612-619</ispartof><rights>2008 Elsevier B.V.</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-1169a49e67d118ac52358bc313f7e694f14459e7ef7f994e89f304aa424373543</citedby><cites>FETCH-LOGICAL-c421t-1169a49e67d118ac52358bc313f7e694f14459e7ef7f994e89f304aa424373543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.dnarep.2008.12.011$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21495464$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19179120$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cao, Zheng</creatorcontrib><creatorcontrib>Julin, Douglas A.</creatorcontrib><title>Characterization in vitro and in vivo of the DNA helicase encoded by Deinococcus radiodurans locus DR1572</title><title>DNA repair</title><addtitle>DNA Repair (Amst)</addtitle><description>Deinococcus radiodurans survives extremely high doses of ionizing and ultraviolet radiation and treatment with various DNA-damaging chemicals. As an effort to identify and characterize proteins that function in DNA repair in this organism, we have studied the protein encoded by locus DR1572. This gene is predicted to encode a Superfamily I DNA helicase, except that genome sequencing indicated that it has a one-base frameshift and would not encode a complete helicase. We have cloned the gene from two different
D. radiodurans strains and find that the frameshift mutation is not present. The corrected gene encodes a 755 residue protein that is similar to the
Bacillus subtilis YvgS protein and to helicase IV of
Escherichia coli. The purified protein (helicase IV
Dr) has ATP hydrolysis and DNA helicase activity. A truncated protein that lacks 214 residues from the N-terminus, which precede the conserved helicase domain, has greater ATPase activity than the full-length protein but has no detectable helicase activity. Disruption of locus DR1572 in the
D. radiodurans chromosome causes greater sensitivity to hydrogen peroxide and methyl-methanesulfonate compared to wild-type cells, but no change in resistance to gamma and ultraviolet radiation and to mitomycin C. The results indicate that locus DR1572 encodes a complete protein that contributes to DNA metabolism in
D. radiodurans.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Antineoplastic Agents, Alkylating - pharmacology</subject><subject>Bacillus subtilis</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Southern</subject><subject>Cloning, Molecular</subject><subject>Deinococcus - enzymology</subject><subject>Deinococcus - genetics</subject><subject>Deinococcus radiodurans</subject><subject>DNA damage</subject><subject>DNA Damage - drug effects</subject><subject>DNA Damage - radiation effects</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - metabolism</subject><subject>DNA repair</subject><subject>DNA Repair - drug effects</subject><subject>DNA Repair - radiation effects</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gamma Rays</subject><subject>Growth, nutrition, cell differenciation</subject><subject>Helicase IV</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Hydrolysis - drug effects</subject><subject>Hydrolysis - radiation effects</subject><subject>In Vitro Techniques</subject><subject>Methyl Methanesulfonate - pharmacology</subject><subject>Microbiology</subject><subject>Mitomycin - pharmacology</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis. Repair</subject><subject>Mutation - genetics</subject><subject>Nucleic Acid Synthesis Inhibitors - pharmacology</subject><subject>Oxidants - pharmacology</subject><subject>Polymerase Chain Reaction</subject><subject>RecF pathway</subject><subject>Sequence Homology, Amino Acid</subject><subject>Ultraviolet Rays</subject><issn>1568-7864</issn><issn>1568-7856</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtqGzEUQEVoyav5g1C0aXee6mokzWgTCHabFkILIV0LWbrCMuORK80Y0q_vmDHJrqv74NwHh5BbYBUwUF-2le9txn3FGWsr4BUDOCOXIFW7aFqp3r3mSlyQq1K2jIFslDonF6Ch0cDZJYnLjc3WDZjjXzvE1NPY00MccqK293NxSDQFOmyQrn7e0w120dmCFHuXPHq6fqErjH1yybmx0Gx9TH7Mti-0S8fO6mm6yz-Q98F2BW9O8Zr8_vb1efl98fjr4cfy_nHhBIdhAaC0FRpV4wFa6ySvZbt2NdShQaVFACGkxgZDE7QW2OpQM2Gt4KJuainqa_J53rvP6c-IZTC7WBx2ne0xjcVwJkEpDRMoZtDlVErGYPY57mx-McDMUbHZmlmxOSo2wM2keBr7eNo_rnfo34ZOTifg0wmwxdkuTCZcLK8cB6GlUMdH72YOJxuHiNkUFyep6GNGNxif4v8_-QdtIppF</recordid><startdate>20090501</startdate><enddate>20090501</enddate><creator>Cao, Zheng</creator><creator>Julin, Douglas A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20090501</creationdate><title>Characterization in vitro and in vivo of the DNA helicase encoded by Deinococcus radiodurans locus DR1572</title><author>Cao, Zheng ; Julin, Douglas A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-1169a49e67d118ac52358bc313f7e694f14459e7ef7f994e89f304aa424373543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Antineoplastic Agents, Alkylating - pharmacology</topic><topic>Bacillus subtilis</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Southern</topic><topic>Cloning, Molecular</topic><topic>Deinococcus - enzymology</topic><topic>Deinococcus - genetics</topic><topic>Deinococcus radiodurans</topic><topic>DNA damage</topic><topic>DNA Damage - drug effects</topic><topic>DNA Damage - radiation effects</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - metabolism</topic><topic>DNA repair</topic><topic>DNA Repair - drug effects</topic><topic>DNA Repair - radiation effects</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gamma Rays</topic><topic>Growth, nutrition, cell differenciation</topic><topic>Helicase IV</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Hydrolysis - drug effects</topic><topic>Hydrolysis - radiation effects</topic><topic>In Vitro Techniques</topic><topic>Methyl Methanesulfonate - pharmacology</topic><topic>Microbiology</topic><topic>Mitomycin - pharmacology</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis. Repair</topic><topic>Mutation - genetics</topic><topic>Nucleic Acid Synthesis Inhibitors - pharmacology</topic><topic>Oxidants - pharmacology</topic><topic>Polymerase Chain Reaction</topic><topic>RecF pathway</topic><topic>Sequence Homology, Amino Acid</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cao, Zheng</creatorcontrib><creatorcontrib>Julin, Douglas A.</creatorcontrib><collection>Pascal-Francis</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>DNA repair</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cao, Zheng</au><au>Julin, Douglas A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization in vitro and in vivo of the DNA helicase encoded by Deinococcus radiodurans locus DR1572</atitle><jtitle>DNA repair</jtitle><addtitle>DNA Repair (Amst)</addtitle><date>2009-05-01</date><risdate>2009</risdate><volume>8</volume><issue>5</issue><spage>612</spage><epage>619</epage><pages>612-619</pages><issn>1568-7864</issn><eissn>1568-7856</eissn><abstract>Deinococcus radiodurans survives extremely high doses of ionizing and ultraviolet radiation and treatment with various DNA-damaging chemicals. As an effort to identify and characterize proteins that function in DNA repair in this organism, we have studied the protein encoded by locus DR1572. This gene is predicted to encode a Superfamily I DNA helicase, except that genome sequencing indicated that it has a one-base frameshift and would not encode a complete helicase. We have cloned the gene from two different
D. radiodurans strains and find that the frameshift mutation is not present. The corrected gene encodes a 755 residue protein that is similar to the
Bacillus subtilis YvgS protein and to helicase IV of
Escherichia coli. The purified protein (helicase IV
Dr) has ATP hydrolysis and DNA helicase activity. A truncated protein that lacks 214 residues from the N-terminus, which precede the conserved helicase domain, has greater ATPase activity than the full-length protein but has no detectable helicase activity. Disruption of locus DR1572 in the
D. radiodurans chromosome causes greater sensitivity to hydrogen peroxide and methyl-methanesulfonate compared to wild-type cells, but no change in resistance to gamma and ultraviolet radiation and to mitomycin C. The results indicate that locus DR1572 encodes a complete protein that contributes to DNA metabolism in
D. radiodurans.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>19179120</pmid><doi>10.1016/j.dnarep.2008.12.011</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 1568-7864 |
| ispartof | DNA repair, 2009-05, Vol.8 (5), p.612-619 |
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| subjects | Adenosine Triphosphate - metabolism Amino Acid Sequence Antineoplastic Agents, Alkylating - pharmacology Bacillus subtilis Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Blotting, Southern Cloning, Molecular Deinococcus - enzymology Deinococcus - genetics Deinococcus radiodurans DNA damage DNA Damage - drug effects DNA Damage - radiation effects DNA Helicases - genetics DNA Helicases - metabolism DNA repair DNA Repair - drug effects DNA Repair - radiation effects Escherichia coli Fundamental and applied biological sciences. Psychology Gamma Rays Growth, nutrition, cell differenciation Helicase IV Hydrogen Peroxide - pharmacology Hydrolysis - drug effects Hydrolysis - radiation effects In Vitro Techniques Methyl Methanesulfonate - pharmacology Microbiology Mitomycin - pharmacology Molecular and cellular biology Molecular genetics Molecular Sequence Data Mutagenesis. Repair Mutation - genetics Nucleic Acid Synthesis Inhibitors - pharmacology Oxidants - pharmacology Polymerase Chain Reaction RecF pathway Sequence Homology, Amino Acid Ultraviolet Rays |
| title | Characterization in vitro and in vivo of the DNA helicase encoded by Deinococcus radiodurans locus DR1572 |
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