Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-template
Identifieur interne : 004907 ( Main/Exploration ); précédent : 004906; suivant : 004908Protein-DNA cross-linking demonstrates stepwise ATP-dependent assembly of T4 DNA polymerase and its accessory proteins on the primer-template
Auteurs : Todd L. Capson [États-Unis] ; Stephen J. Benkovic [États-Unis] ; Nancy G. Nossal [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1991.
English descriptors
- Teeft :
- Accessory, Accessory protein, Accessory proteins, Adduct, Atpase, Atpys, Bacteriophage, Biol, Chem, Datp, Dctp, Dgtp, Dntp, Dttp, Duplex, Exonuclease, Exonuclease activity, Nossal, Polymerase, Polymerase accessory proteins, Primer, Primer terminus, Processive, Processive synthesis, Protein, Reaction mixtures, Replication, Replication proteins, Replication system, Room temperature, Terminus.
Abstract
Abstract: T4 DNA polymerase, the 44 62 and 45 polymerase accessory proteins, and 32 single-stranded DNA-binding protein catalyze ATP-dependent DNA synthesis. Using DNA primers with cross-linkable residues at specific positions, we obtained structural data that reveal how these proteins assemble on the primer-template. With the nonhydrolyzable ATP analog ATPγS, assembly of the 44 62 and 45 proteins on the primer requires 32 protein but not polymerase. ATP hydrolysis changes the position and intensity of cross-linking to each of the accessory proteins and allows cross-linking of polymerase. Our data indicate that the initial binding of the three accessory proteins and ATP to a 32 protein-covered primer-template is followed by ATP hydrolysis, binding of polymerase, and movement of the accessory proteins to yield a complex capable of processive DNA synthesis.
Url:
DOI: 10.1016/0092-8674(91)90159-V
Affiliations:
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Capson</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Chemistry Pennsylvania State University University Park</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>† Present address: National Institutes of Health, Building 8, Room 2A-15, Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Benkovic, Stephen J" sort="Benkovic, Stephen J" uniqKey="Benkovic S" first="Stephen J." last="Benkovic">Stephen J. Benkovic</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Chemistry Pennsylvania State University University Park</wicri:cityArea></affiliation></author><author><name sortKey="Nossal, Nancy G" sort="Nossal, Nancy G" uniqKey="Nossal N" first="Nancy G." last="Nossal">Nancy G. Nossal</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Section on Nucleic Acid Biochemistry Laboratory of Biochemical Pharmacology National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health Bethesda</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">65</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="249">249</biblScope><biblScope unit="page" to="258">258</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Accessory</term><term>Accessory protein</term><term>Accessory proteins</term><term>Adduct</term><term>Atpase</term><term>Atpys</term><term>Bacteriophage</term><term>Biol</term><term>Chem</term><term>Datp</term><term>Dctp</term><term>Dgtp</term><term>Dntp</term><term>Dttp</term><term>Duplex</term><term>Exonuclease</term><term>Exonuclease activity</term><term>Nossal</term><term>Polymerase</term><term>Polymerase accessory proteins</term><term>Primer</term><term>Primer terminus</term><term>Processive</term><term>Processive synthesis</term><term>Protein</term><term>Reaction mixtures</term><term>Replication</term><term>Replication proteins</term><term>Replication system</term><term>Room temperature</term><term>Terminus</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: T4 DNA polymerase, the 44 62 and 45 polymerase accessory proteins, and 32 single-stranded DNA-binding protein catalyze ATP-dependent DNA synthesis. Using DNA primers with cross-linkable residues at specific positions, we obtained structural data that reveal how these proteins assemble on the primer-template. With the nonhydrolyzable ATP analog ATPγS, assembly of the 44 62 and 45 proteins on the primer requires 32 protein but not polymerase. ATP hydrolysis changes the position and intensity of cross-linking to each of the accessory proteins and allows cross-linking of polymerase. Our data indicate that the initial binding of the three accessory proteins and ATP to a 32 protein-covered primer-template is followed by ATP hydrolysis, binding of polymerase, and movement of the accessory proteins to yield a complex capable of processive DNA synthesis.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li><li>Pennsylvanie</li></region></list><tree><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Capson, Todd L" sort="Capson, Todd L" uniqKey="Capson T" first="Todd L." last="Capson">Todd L. Capson</name></region><name sortKey="Benkovic, Stephen J" sort="Benkovic, Stephen J" uniqKey="Benkovic S" first="Stephen J." last="Benkovic">Stephen J. Benkovic</name><name sortKey="Capson, Todd L" sort="Capson, Todd L" uniqKey="Capson T" first="Todd L." last="Capson">Todd L. Capson</name><name sortKey="Nossal, Nancy G" sort="Nossal, Nancy G" uniqKey="Nossal N" first="Nancy G." last="Nossal">Nancy G. 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