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rdf:type |
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lifeskim:mentions |
umls-concept:C0012892,
umls-concept:C0162570,
umls-concept:C0175721,
umls-concept:C0204514,
umls-concept:C0392747,
umls-concept:C0439855,
umls-concept:C1152375,
umls-concept:C1704675,
umls-concept:C1706853,
umls-concept:C1708715,
umls-concept:C1879748,
umls-concept:C2346689
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pubmed:issue |
50
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pubmed:dateCreated |
1998-1-15
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pubmed:abstractText |
A multisubunit ring-shaped protein complex is used to tether the polymerase to the DNA at the primer-template junction in most DNA replication systems. This "sliding clamp" interacts with the polymerase, completely encircles the DNA duplex, and is assembled onto the DNA by a specific clamp loading complex in an ATP-driven process. Site-specific mutagenesis has been used to introduce single cysteine residues as reactive sites for adduct formation within each of the three subunits of the bacteriophage T4-coded sliding clamp complex (gp45). Two such mutants, gp45S19C and gp45K81C, are reacted with the cysteine-specific photoactivable cross-linker TFPAM-3 and used to track the changes in the relative positioning of the gp45 subunits with one another and with the other components of the clamp loading complex (gp44/62) in the various stages of the loading process. Cross-linking interactions performed in the presence of nucleotide cofactors show that ATP binding and hydrolysis, interaction with primer-template DNA, and release of ADP all result in significant conformational changes within the clamp loading cycle. A structural model is presented to account for the observed rearrangements of intersubunit contacts within the complex during the loading process.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorobenzenes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/N-(4-azido-2,3,5,6-tetrafluorobenzyl...,
http://linkedlifedata.com/resource/pubmed/chemical/T7C-45 protein, Bacteriophage T4,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gene 44 protein, Enterobacteria...,
http://linkedlifedata.com/resource/pubmed/chemical/gene 45 protein, Enterobacteria...,
http://linkedlifedata.com/resource/pubmed/chemical/gp62 protein, bacteriophage T4
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31666-76
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9395508-Adenosine Triphosphate,
pubmed-meshheading:9395508-Binding Sites,
pubmed-meshheading:9395508-Cross-Linking Reagents,
pubmed-meshheading:9395508-DNA Replication,
pubmed-meshheading:9395508-DNA-Directed DNA Polymerase,
pubmed-meshheading:9395508-Fluorobenzenes,
pubmed-meshheading:9395508-Macromolecular Substances,
pubmed-meshheading:9395508-Maleimides,
pubmed-meshheading:9395508-Models, Chemical,
pubmed-meshheading:9395508-Models, Molecular,
pubmed-meshheading:9395508-Mutagenesis, Site-Directed,
pubmed-meshheading:9395508-Photochemistry,
pubmed-meshheading:9395508-Protein Conformation,
pubmed-meshheading:9395508-T-Phages,
pubmed-meshheading:9395508-Trans-Activators,
pubmed-meshheading:9395508-Viral Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. I. Conformational changes within the gp44/62-gp45-ATP complex during clamp loading.
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pubmed:affiliation |
Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon 97403-1229, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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