The structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction protein.
Identifieur interne : 000806 ( Main/Exploration ); précédent : 000805; suivant : 000807The structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction protein.
Auteurs : Christopher K. Kennaway [Royaume-Uni] ; Agnieszka Obarska-Kosinska ; John H. White ; Irina Tuszynska ; Laurie P. Cooper ; Janusz M. Bujnicki ; John Trinick ; David T F. DrydenSource :
- Nucleic acids research [ 1362-4962 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : DNA, Site-Specific DNA-Methyltransferase (Adenine-Specific), Viral Proteins.
- enzymology : Escherichia coli.
- chemical , ultrastructure : Site-Specific DNA-Methyltransferase (Adenine-Specific), Viral Proteins.
- Models, Molecular, Molecular Mimicry.
Abstract
Type-I DNA restriction-modification (R/M) systems are important agents in limiting the transmission of mobile genetic elements responsible for spreading bacterial resistance to antibiotics. EcoKI, a Type I R/M enzyme from Escherichia coli, acts by methylation- and sequence-specific recognition, leading to either methylation of DNA or translocation and cutting at a random site, often hundreds of base pairs away. Consisting of one specificity subunit, two modification subunits, and two DNA translocase/endonuclease subunits, EcoKI is inhibited by the T7 phage antirestriction protein ocr, a DNA mimic. We present a 3D density map generated by negative-stain electron microscopy and single particle analysis of the central core of the restriction complex, the M.EcoKI M(2)S(1) methyltransferase, bound to ocr. We also present complete atomic models of M.EcoKI in complex with ocr and its cognate DNA giving a clear picture of the overall clamp-like operation of the enzyme. The model is consistent with a large body of experimental data on EcoKI published over 40 years.
DOI: 10.1093/nar/gkn988
PubMed: 19074193
Affiliations:
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White</name></author><author><name sortKey="Tuszynska, Irina" sort="Tuszynska, Irina" uniqKey="Tuszynska I" first="Irina" last="Tuszynska">Irina Tuszynska</name></author><author><name sortKey="Cooper, Laurie P" sort="Cooper, Laurie P" uniqKey="Cooper L" first="Laurie P" last="Cooper">Laurie P. Cooper</name></author><author><name sortKey="Bujnicki, Janusz M" sort="Bujnicki, Janusz M" uniqKey="Bujnicki J" first="Janusz M" last="Bujnicki">Janusz M. Bujnicki</name></author><author><name sortKey="Trinick, John" sort="Trinick, John" uniqKey="Trinick J" first="John" last="Trinick">John Trinick</name></author><author><name sortKey="Dryden, David T F" sort="Dryden, David T F" uniqKey="Dryden D" first="David T F" last="Dryden">David T F. 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Kennaway</name><affiliation wicri:level="4"><nlm:affiliation>Astbury Centre, Institute of Molecular and Cellular Biology, University of Leeds, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Astbury Centre, Institute of Molecular and Cellular Biology, University of Leeds</wicri:regionArea><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName><orgName type="university">Université de Leeds</orgName></affiliation></author><author><name sortKey="Obarska Kosinska, Agnieszka" sort="Obarska Kosinska, Agnieszka" uniqKey="Obarska Kosinska A" first="Agnieszka" last="Obarska-Kosinska">Agnieszka Obarska-Kosinska</name></author><author><name sortKey="White, John H" sort="White, John H" uniqKey="White J" first="John H" last="White">John H. White</name></author><author><name sortKey="Tuszynska, Irina" sort="Tuszynska, Irina" uniqKey="Tuszynska I" first="Irina" last="Tuszynska">Irina Tuszynska</name></author><author><name sortKey="Cooper, Laurie P" sort="Cooper, Laurie P" uniqKey="Cooper L" first="Laurie P" last="Cooper">Laurie P. Cooper</name></author><author><name sortKey="Bujnicki, Janusz M" sort="Bujnicki, Janusz M" uniqKey="Bujnicki J" first="Janusz M" last="Bujnicki">Janusz M. Bujnicki</name></author><author><name sortKey="Trinick, John" sort="Trinick, John" uniqKey="Trinick J" first="John" last="Trinick">John Trinick</name></author><author><name sortKey="Dryden, David T F" sort="Dryden, David T F" uniqKey="Dryden D" first="David T F" last="Dryden">David T F. Dryden</name></author></analytic><series><title level="j">Nucleic acids research</title><idno type="eISSN">1362-4962</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>DNA (chemistry)</term><term>Escherichia coli (enzymology)</term><term>Models, Molecular</term><term>Molecular Mimicry</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific) (chemistry)</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific) (ultrastructure)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA</term><term>Site-Specific DNA-Methyltransferase (Adenine-Specific)</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Site-Specific DNA-Methyltransferase (Adenine-Specific)</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Molecular Mimicry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Type-I DNA restriction-modification (R/M) systems are important agents in limiting the transmission of mobile genetic elements responsible for spreading bacterial resistance to antibiotics. EcoKI, a Type I R/M enzyme from Escherichia coli, acts by methylation- and sequence-specific recognition, leading to either methylation of DNA or translocation and cutting at a random site, often hundreds of base pairs away. Consisting of one specificity subunit, two modification subunits, and two DNA translocase/endonuclease subunits, EcoKI is inhibited by the T7 phage antirestriction protein ocr, a DNA mimic. We present a 3D density map generated by negative-stain electron microscopy and single particle analysis of the central core of the restriction complex, the M.EcoKI M(2)S(1) methyltransferase, bound to ocr. We also present complete atomic models of M.EcoKI in complex with ocr and its cognate DNA giving a clear picture of the overall clamp-like operation of the enzyme. The model is consistent with a large body of experimental data on EcoKI published over 40 years.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Yorkshire-et-Humber</li></region><settlement><li>Leeds</li></settlement><orgName><li>Université de Leeds</li></orgName></list><tree><noCountry><name sortKey="Bujnicki, Janusz M" sort="Bujnicki, Janusz M" uniqKey="Bujnicki J" first="Janusz M" last="Bujnicki">Janusz M. Bujnicki</name><name sortKey="Cooper, Laurie P" sort="Cooper, Laurie P" uniqKey="Cooper L" first="Laurie P" last="Cooper">Laurie P. Cooper</name><name sortKey="Dryden, David T F" sort="Dryden, David T F" uniqKey="Dryden D" first="David T F" last="Dryden">David T F. Dryden</name><name sortKey="Obarska Kosinska, Agnieszka" sort="Obarska Kosinska, Agnieszka" uniqKey="Obarska Kosinska A" first="Agnieszka" last="Obarska-Kosinska">Agnieszka Obarska-Kosinska</name><name sortKey="Trinick, John" sort="Trinick, John" uniqKey="Trinick J" first="John" last="Trinick">John Trinick</name><name sortKey="Tuszynska, Irina" sort="Tuszynska, Irina" uniqKey="Tuszynska I" first="Irina" last="Tuszynska">Irina Tuszynska</name><name sortKey="White, John H" sort="White, John H" uniqKey="White J" first="John H" last="White">John H. White</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Kennaway, Christopher K" sort="Kennaway, Christopher K" uniqKey="Kennaway C" first="Christopher K" last="Kennaway">Christopher K. Kennaway</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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