IronSulferCluV1, Main, Exploration, bibRecord, 000202

Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.

Identifieur interne : 000202 ( Main/Exploration ); précédent : 000201; suivant : 000203

Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.

Auteurs : Ning Jia [États-Unis] ; Mihaela C. Unciuleac [États-Unis] ; Chaoyou Xue [États-Unis] ; Eric C. Greene [États-Unis] ; Dinshaw J. Patel [États-Unis] ; Stewart Shuman [États-Unis]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2019.

RBID : pubmed:31740608

Descripteurs français

English descriptors

KwdEn :
- Adenosine Triphosphate (metabolism), Adenylyl Imidodiphosphate (metabolism), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Binding Sites (MeSH), Catalytic Domain (MeSH), Cryoelectron Microscopy (MeSH), DNA Breaks, Double-Stranded (MeSH), DNA, Single-Stranded (metabolism), Endodeoxyribonucleases (chemistry), Endodeoxyribonucleases (genetics), Endodeoxyribonucleases (metabolism), Hydrolysis (MeSH), Iron-Sulfur Proteins (chemistry), Models, Molecular (MeSH), Mutation (MeSH), Mycobacterium smegmatis (chemistry), Mycobacterium smegmatis (genetics), Nucleic Acid Heteroduplexes (MeSH), Protein Domains (MeSH), Single Molecule Imaging (MeSH).
MESH :
- chemical , chemistry : Bacterial Proteins, Endodeoxyribonucleases, Iron-Sulfur Proteins.
- chemical , genetics : Bacterial Proteins, Endodeoxyribonucleases.
- chemical , metabolism : Adenosine Triphosphate, Adenylyl Imidodiphosphate, Bacterial Proteins, DNA, Single-Stranded, Endodeoxyribonucleases.
- chemistry : Mycobacterium smegmatis.
- genetics : Mycobacterium smegmatis.
- Binding Sites, Catalytic Domain, Cryoelectron Microscopy, DNA Breaks, Double-Stranded, Hydrolysis, Models, Molecular, Mutation, Nucleic Acid Heteroduplexes, Protein Domains, Single Molecule Imaging.

Abstract

Mycobacterial AdnAB is a heterodimeric helicase-nuclease that initiates homologous recombination by resecting DNA double-strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N-terminal motor domain and a C-terminal nuclease domain. Here we report cryoelectron microscopy (cryo-EM) structures of AdnAB in three functional states: in the absence of DNA and in complex with forked duplex DNAs before and after cleavage of the 5' single-strand DNA (ssDNA) tail by the AdnA nuclease. The structures reveal the path of the 5' ssDNA through the AdnA nuclease domain and the mechanism of 5' strand cleavage; the path of the 3' tracking strand through the AdnB motor and the DNA contacts that couple ATP hydrolysis to mechanical work; the position of the AdnA iron-sulfur cluster subdomain at the Y junction and its likely role in maintaining the split trajectories of the unwound 5' and 3' strands. Single-molecule DNA curtain analysis of DSB resection reveals that AdnAB is highly processive but prone to spontaneous pausing at random sites on duplex DNA. A striking property of AdnAB is that the velocity of DSB resection slows after the enzyme experiences a spontaneous pause. Our results highlight shared as well as distinctive properties of AdnAB vis-à-vis the RecBCD and AddAB clades of bacterial DSB-resecting motor nucleases.

DOI: 10.1073/pnas.1913546116
PubMed: 31740608
PubMed Central: PMC6900545

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000193
to stream Main, to step Curation: 000193

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.</title>
<author><name sortKey="Jia, Ning" sort="Jia, Ning" uniqKey="Jia N" first="Ning" last="Jia">Ning Jia</name>
<affiliation wicri:level="2"><nlm:affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Structural Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Unciuleac, Mihaela C" sort="Unciuleac, Mihaela C" uniqKey="Unciuleac M" first="Mihaela C" last="Unciuleac">Mihaela C. Unciuleac</name>
<affiliation wicri:level="2"><nlm:affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Molecular Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Xue, Chaoyou" sort="Xue, Chaoyou" uniqKey="Xue C" first="Chaoyou" last="Xue">Chaoyou Xue</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Columbia University, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Greene, Eric C" sort="Greene, Eric C" uniqKey="Greene E" first="Eric C" last="Greene">Eric C. Greene</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Columbia University, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Patel, Dinshaw J" sort="Patel, Dinshaw J" uniqKey="Patel D" first="Dinshaw J" last="Patel">Dinshaw J. Patel</name>
<affiliation wicri:level="2"><nlm:affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Structural Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Shuman, Stewart" sort="Shuman, Stewart" uniqKey="Shuman S" first="Stewart" last="Shuman">Stewart Shuman</name>
<affiliation wicri:level="2"><nlm:affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Molecular Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2019">2019</date>
<idno type="RBID">pubmed:31740608</idno>
<idno type="pmid">31740608</idno>
<idno type="doi">10.1073/pnas.1913546116</idno>
<idno type="pmc">PMC6900545</idno>
<idno type="wicri:Area/Main/Corpus">000193</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000193</idno>
<idno type="wicri:Area/Main/Curation">000193</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000193</idno>
<idno type="wicri:Area/Main/Exploration">000193</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.</title>
<author><name sortKey="Jia, Ning" sort="Jia, Ning" uniqKey="Jia N" first="Ning" last="Jia">Ning Jia</name>
<affiliation wicri:level="2"><nlm:affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Structural Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Unciuleac, Mihaela C" sort="Unciuleac, Mihaela C" uniqKey="Unciuleac M" first="Mihaela C" last="Unciuleac">Mihaela C. Unciuleac</name>
<affiliation wicri:level="2"><nlm:affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Molecular Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Xue, Chaoyou" sort="Xue, Chaoyou" uniqKey="Xue C" first="Chaoyou" last="Xue">Chaoyou Xue</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Columbia University, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Greene, Eric C" sort="Greene, Eric C" uniqKey="Greene E" first="Eric C" last="Greene">Eric C. Greene</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Columbia University, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Patel, Dinshaw J" sort="Patel, Dinshaw J" uniqKey="Patel D" first="Dinshaw J" last="Patel">Dinshaw J. Patel</name>
<affiliation wicri:level="2"><nlm:affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Structural Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Shuman, Stewart" sort="Shuman, Stewart" uniqKey="Shuman S" first="Stewart" last="Shuman">Stewart Shuman</name>
<affiliation wicri:level="2"><nlm:affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Molecular Biology Program, Sloan Kettering Institute, New York</wicri:cityArea>
</affiliation>
</author>
</analytic>
<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
<idno type="eISSN">1091-6490</idno>
<imprint><date when="2019" type="published">2019</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphate (metabolism)</term>
<term>Adenylyl Imidodiphosphate (metabolism)</term>
<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Binding Sites (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Cryoelectron Microscopy (MeSH)</term>
<term>DNA Breaks, Double-Stranded (MeSH)</term>
<term>DNA, Single-Stranded (metabolism)</term>
<term>Endodeoxyribonucleases (chemistry)</term>
<term>Endodeoxyribonucleases (genetics)</term>
<term>Endodeoxyribonucleases (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Mycobacterium smegmatis (chemistry)</term>
<term>Mycobacterium smegmatis (genetics)</term>
<term>Nucleic Acid Heteroduplexes (MeSH)</term>
<term>Protein Domains (MeSH)</term>
<term>Single Molecule Imaging (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN simple brin (métabolisme)</term>
<term>Adenylyl imidodiphosphate (métabolisme)</term>
<term>Adénosine triphosphate (métabolisme)</term>
<term>Cassures double-brin de l'ADN (MeSH)</term>
<term>Cryomicroscopie électronique (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Endodeoxyribonucleases (composition chimique)</term>
<term>Endodeoxyribonucleases (génétique)</term>
<term>Endodeoxyribonucleases (métabolisme)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Hétéroduplexes d'acides nucléiques (MeSH)</term>
<term>Imagerie de molécules uniques (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Mycobacterium smegmatis (composition chimique)</term>
<term>Mycobacterium smegmatis (génétique)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term>
<term>Endodeoxyribonucleases</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term>
<term>Endodeoxyribonucleases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphate</term>
<term>Adenylyl Imidodiphosphate</term>
<term>Bacterial Proteins</term>
<term>DNA, Single-Stranded</term>
<term>Endodeoxyribonucleases</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Mycobacterium smegmatis</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Endodeoxyribonucleases</term>
<term>Ferrosulfoprotéines</term>
<term>Mycobacterium smegmatis</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mycobacterium smegmatis</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Endodeoxyribonucleases</term>
<term>Mycobacterium smegmatis</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN simple brin</term>
<term>Adenylyl imidodiphosphate</term>
<term>Adénosine triphosphate</term>
<term>Endodeoxyribonucleases</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Catalytic Domain</term>
<term>Cryoelectron Microscopy</term>
<term>DNA Breaks, Double-Stranded</term>
<term>Hydrolysis</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Nucleic Acid Heteroduplexes</term>
<term>Protein Domains</term>
<term>Single Molecule Imaging</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cassures double-brin de l'ADN</term>
<term>Cryomicroscopie électronique</term>
<term>Domaine catalytique</term>
<term>Domaines protéiques</term>
<term>Hydrolyse</term>
<term>Hétéroduplexes d'acides nucléiques</term>
<term>Imagerie de molécules uniques</term>
<term>Modèles moléculaires</term>
<term>Mutation</term>
<term>Sites de fixation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Mycobacterial AdnAB is a heterodimeric helicase-nuclease that initiates homologous recombination by resecting DNA double-strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N-terminal motor domain and a C-terminal nuclease domain. Here we report cryoelectron microscopy (cryo-EM) structures of AdnAB in three functional states: in the absence of DNA and in complex with forked duplex DNAs before and after cleavage of the 5' single-strand DNA (ssDNA) tail by the AdnA nuclease. The structures reveal the path of the 5' ssDNA through the AdnA nuclease domain and the mechanism of 5' strand cleavage; the path of the 3' tracking strand through the AdnB motor and the DNA contacts that couple ATP hydrolysis to mechanical work; the position of the AdnA iron-sulfur cluster subdomain at the Y junction and its likely role in maintaining the split trajectories of the unwound 5' and 3' strands. Single-molecule DNA curtain analysis of DSB resection reveals that AdnAB is highly processive but prone to spontaneous pausing at random sites on duplex DNA. A striking property of AdnAB is that the velocity of DSB resection slows after the enzyme experiences a spontaneous pause. Our results highlight shared as well as distinctive properties of AdnAB vis-à-vis the RecBCD and AddAB clades of bacterial DSB-resecting motor nucleases.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31740608</PMID>
<DateCompleted><Year>2020</Year>
<Month>04</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>05</Month>
<Day>19</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>116</Volume>
<Issue>49</Issue>
<PubDate><Year>2019</Year>
<Month>12</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.</ArticleTitle>
<Pagination><MedlinePgn>24507-24516</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1913546116</ELocationID>
<Abstract><AbstractText>Mycobacterial AdnAB is a heterodimeric helicase-nuclease that initiates homologous recombination by resecting DNA double-strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N-terminal motor domain and a C-terminal nuclease domain. Here we report cryoelectron microscopy (cryo-EM) structures of AdnAB in three functional states: in the absence of DNA and in complex with forked duplex DNAs before and after cleavage of the 5' single-strand DNA (ssDNA) tail by the AdnA nuclease. The structures reveal the path of the 5' ssDNA through the AdnA nuclease domain and the mechanism of 5' strand cleavage; the path of the 3' tracking strand through the AdnB motor and the DNA contacts that couple ATP hydrolysis to mechanical work; the position of the AdnA iron-sulfur cluster subdomain at the Y junction and its likely role in maintaining the split trajectories of the unwound 5' and 3' strands. Single-molecule DNA curtain analysis of DSB resection reveals that AdnAB is highly processive but prone to spontaneous pausing at random sites on duplex DNA. A striking property of AdnAB is that the velocity of DSB resection slows after the enzyme experiences a spontaneous pause. Our results highlight shared as well as distinctive properties of AdnAB vis-à-vis the RecBCD and AddAB clades of bacterial DSB-resecting motor nucleases.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jia</LastName>
<ForeName>Ning</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Unciuleac</LastName>
<ForeName>Mihaela C</ForeName>
<Initials>MC</Initials>
<AffiliationInfo><Affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xue</LastName>
<ForeName>Chaoyou</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Greene</LastName>
<ForeName>Eric C</ForeName>
<Initials>EC</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Patel</LastName>
<ForeName>Dinshaw J</ForeName>
<Initials>DJ</Initials>
<AffiliationInfo><Affiliation>Structural Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shuman</LastName>
<ForeName>Stewart</ForeName>
<Initials>S</Initials>
<Identifier Source="ORCID">0000-0001-5034-6438</Identifier>
<AffiliationInfo><Affiliation>Molecular Biology Program, Sloan Kettering Institute, New York, NY 10065; pateld@mskcc.org s-shuman@ski.mskcc.org.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>6PPJ</AccessionNumber>
<AccessionNumber>6PPR</AccessionNumber>
<AccessionNumber>6PPU</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<GrantList CompleteYN="Y"><Grant><GrantID>P30 CA008748</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 AI064693</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R35 GM118026</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R35 GM126945</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>11</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004277">DNA, Single-Stranded</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D009692">Nucleic Acid Heteroduplexes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>25612-73-1</RegistryNumber>
<NameOfSubstance UI="D000266">Adenylyl Imidodiphosphate</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber>
<NameOfSubstance UI="D000255">Adenosine Triphosphate</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
<NameOfSubstance UI="D004706">Endodeoxyribonucleases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000255" MajorTopicYN="N">Adenosine Triphosphate</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000266" MajorTopicYN="N">Adenylyl Imidodiphosphate</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020285" MajorTopicYN="N">Cryoelectron Microscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053903" MajorTopicYN="Y">DNA Breaks, Double-Stranded</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004277" MajorTopicYN="N">DNA, Single-Stranded</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004706" MajorTopicYN="N">Endodeoxyribonucleases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020102" MajorTopicYN="N">Mycobacterium smegmatis</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009692" MajorTopicYN="N">Nucleic Acid Heteroduplexes</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072760" MajorTopicYN="N">Single Molecule Imaging</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">DNA curtain</Keyword>
<Keyword MajorTopicYN="Y">DNA end resection</Keyword>
<Keyword MajorTopicYN="Y">cryoelectron microscopy</Keyword>
<Keyword MajorTopicYN="Y">homologous recombination</Keyword>
</KeywordList>
<CoiStatement>The authors declare no competing interest.</CoiStatement>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year>
<Month>11</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2020</Year>
<Month>4</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2019</Year>
<Month>11</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">31740608</ArticleId>
<ArticleId IdType="pii">1913546116</ArticleId>
<ArticleId IdType="doi">10.1073/pnas.1913546116</ArticleId>
<ArticleId IdType="pmc">PMC6900545</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Mol Microbiol. 2002 Feb;43(4):823-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11929535</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>BMC Struct Biol. 2005 Jun 28;5:9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15985153</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Elife. 2016 Sep 20;5:</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27644322</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 2008 Feb 15;22(4):512-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18281464</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 2016 Jun;41(6):491-507</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27156117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2010 Jun;38(11):3721-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20185564</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2014 Apr 17;508(7496):416-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24670664</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2013 Jan;11(1):9-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23202527</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2008 Aug 20;27(16):2222-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18668125</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>DNA Repair (Amst). 2014 Aug;20:119-129</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24569169</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2011 Mar;39(6):2271-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21071401</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Aug 22;500(7463):482-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23851395</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2017 Jan 25;45(2):762-774</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27899634</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2007 Nov 16;131(4):694-705</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18022364</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2001 Jan 18;409(6818):370-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11201749</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2003 Sep 5;114(5):647-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13678587</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Microbiol Mol Biol Rev. 2008 Dec;72(4):642-71, Table of Contents</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19052323</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2013 Jul 9;110(28):E2562-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23798400</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2001 Jan 18;409(6818):374-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11201750</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Bacteriol. 2015 Oct;197(19):3121-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26195593</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2010 Dec 16;468(7326):983-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21107319</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2010 Jan 22;285(4):2632-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19920138</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Cell Biol. 2014;123:217-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24974030</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2012 Mar 21;31(6):1568-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22307084</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Microbiol. 2011 Jan;79(2):316-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21219454</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 2009 Jun 15;23(12):1423-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19470566</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2004 Nov 11;432(7014):187-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15538360</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2010 Nov 5;285(45):34319-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20736178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2006 Dec 29;127(7):1349-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17190599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2007 Aug 3;371(1):66-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17570399</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>État de New York</li>
</region>
</list>
<tree><country name="États-Unis"><region name="État de New York"><name sortKey="Jia, Ning" sort="Jia, Ning" uniqKey="Jia N" first="Ning" last="Jia">Ning Jia</name>
</region>
<name sortKey="Greene, Eric C" sort="Greene, Eric C" uniqKey="Greene E" first="Eric C" last="Greene">Eric C. Greene</name>
<name sortKey="Patel, Dinshaw J" sort="Patel, Dinshaw J" uniqKey="Patel D" first="Dinshaw J" last="Patel">Dinshaw J. Patel</name>
<name sortKey="Shuman, Stewart" sort="Shuman, Stewart" uniqKey="Shuman S" first="Stewart" last="Shuman">Stewart Shuman</name>
<name sortKey="Unciuleac, Mihaela C" sort="Unciuleac, Mihaela C" uniqKey="Unciuleac M" first="Mihaela C" last="Unciuleac">Mihaela C. Unciuleac</name>
<name sortKey="Xue, Chaoyou" sort="Xue, Chaoyou" uniqKey="Xue C" first="Chaoyou" last="Xue">Chaoyou Xue</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/IronSulferCluV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000202 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000202 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    IronSulferCluV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:31740608
   |texte=   Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:31740608" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a IronSulferCluV1

This area was generated with Dilib version V0.6.38.
Data generation: Sat Nov 21 15:13:39 2020. Site generation: Sat Nov 21 15:14:05 2020

	Serveur d'exploration cluster fer-soufre
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration cluster fer-soufre

Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.

Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki