DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster
Conserved Iron-Sulfur (Fe-S) clusters are found in a growing family of metalloproteins that are implicated in prokaryotic and eukaryotic DNA replication and repair. Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases c...
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| Veröffentlicht in: | Nucleic acids research 2012-05, Vol.40 (10), p.4247-4260 |
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| creator | Wu, Yuliang Brosh, Jr, Robert M |
| description | Conserved Iron-Sulfur (Fe-S) clusters are found in a growing family of metalloproteins that are implicated in prokaryotic and eukaryotic DNA replication and repair. Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. We will discuss testable models for how the conserved Fe-S cluster might operate in helicase and helicase-nuclease enzymes to conduct their specialized functions that help to preserve the integrity of the genome. |
| doi_str_mv | 10.1093/nar/gks039 |
| format | Article |
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Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. 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Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. We will discuss testable models for how the conserved Fe-S cluster might operate in helicase and helicase-nuclease enzymes to conduct their specialized functions that help to preserve the integrity of the genome.</description><subject>Amino Acid Sequence</subject><subject>Chromium</subject><subject>Deoxyribonucleases - chemistry</subject><subject>Deoxyribonucleases - metabolism</subject><subject>DNA - metabolism</subject><subject>DNA biosynthesis</subject><subject>DNA Glycosylases - chemistry</subject><subject>DNA helicase</subject><subject>DNA Helicases - chemistry</subject><subject>DNA Helicases - metabolism</subject><subject>DNA Primase - chemistry</subject><subject>DNA repair</subject><subject>Enzymes</subject><subject>Genomes</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Tertiary</subject><subject>Replication</subject><subject>Stress</subject><subject>Structure-function relationships</subject><subject>Survey and Summary</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkctOwzAQRS0EoqWw4QNQlggpdPxIYm-QqvKUKrqBteU6dhtInGInReXrSdVSwY6VNZ6jo5m5CJ1juMYg6NApP5y_B6DiAPUxTUnMREoOUR8oJDEGxnvoJIQ3AMxwwo5RjxDCs5SIPprePo-ihSkLrYKJlMv3RexaXZrNr3Ff68qE6LNoFpGKdO2C8SuTR4WvXRza0rY-0mUbGuNP0ZFVZTBnu3eAXu_vXsaP8WT68DQeTWLNMG5iDcJaqjnLAIgFhS0wLFKbpGkOLE-5AJonqZklGmtBFRCdWKUtY2qWcUXpAN1svct2VplcG9d4VcqlLyrl17JWhfzbccVCzuuVpDTjPBOd4HIn8PVHa0IjqyJoU5bKmboNEgMBzhhh_B8oTrKkO-fGerVFta9D8MbuJ8IgN2HJLiy5DauDL37vsEd_0qHfk52R2A</recordid><startdate>20120501</startdate><enddate>20120501</enddate><creator>Wu, Yuliang</creator><creator>Brosh, Jr, Robert M</creator><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>7X8</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20120501</creationdate><title>DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster</title><author>Wu, Yuliang ; Brosh, Jr, Robert M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-c09ff3c847002f0a1f04196f566d04d68903d56eb5c1c93a02c5facf44ab78a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Chromium</topic><topic>Deoxyribonucleases - chemistry</topic><topic>Deoxyribonucleases - metabolism</topic><topic>DNA - metabolism</topic><topic>DNA biosynthesis</topic><topic>DNA Glycosylases - chemistry</topic><topic>DNA helicase</topic><topic>DNA Helicases - chemistry</topic><topic>DNA Helicases - metabolism</topic><topic>DNA Primase - chemistry</topic><topic>DNA repair</topic><topic>Enzymes</topic><topic>Genomes</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>Iron-Sulfur Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Protein Structure, Tertiary</topic><topic>Replication</topic><topic>Stress</topic><topic>Structure-function relationships</topic><topic>Survey and Summary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Yuliang</creatorcontrib><creatorcontrib>Brosh, Jr, Robert M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Yuliang</au><au>Brosh, Jr, Robert M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2012-05-01</date><risdate>2012</risdate><volume>40</volume><issue>10</issue><spage>4247</spage><epage>4260</epage><pages>4247-4260</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Conserved Iron-Sulfur (Fe-S) clusters are found in a growing family of metalloproteins that are implicated in prokaryotic and eukaryotic DNA replication and repair. Among these are DNA helicase and helicase-nuclease enzymes that preserve chromosomal stability and are genetically linked to diseases characterized by DNA repair defects and/or a poor response to replication stress. Insight to the structural and functional importance of the conserved Fe-S domain in DNA helicases has been gleaned from structural studies of the purified proteins and characterization of Fe-S cluster site-directed mutants. In this review, we will provide a current perspective of what is known about the Fe-S cluster helicases, with an emphasis on how the conserved redox active domain may facilitate mechanistic aspects of helicase function. We will discuss testable models for how the conserved Fe-S cluster might operate in helicase and helicase-nuclease enzymes to conduct their specialized functions that help to preserve the integrity of the genome.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>22287629</pmid><doi>10.1093/nar/gks039</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 2012-05, Vol.40 (10), p.4247-4260 |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Oxford Open; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Chromium Deoxyribonucleases - chemistry Deoxyribonucleases - metabolism DNA - metabolism DNA biosynthesis DNA Glycosylases - chemistry DNA helicase DNA Helicases - chemistry DNA Helicases - metabolism DNA Primase - chemistry DNA repair Enzymes Genomes Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - metabolism Molecular Sequence Data Protein Structure, Tertiary Replication Stress Structure-function relationships Survey and Summary |
| title | DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster |
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