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Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the Bacteriophage T7 Replisome.
Wallen, Jamie R; Zhang, Hao; Weis, Caroline; Cui, Weidong; Foster, Brittni M; Ho, Chris M W; Hammel, Michal; Tainer, John A; Gross, Michael L; Ellenberger, Tom.
Afiliación
  • Wallen JR; Department of Chemistry & Physics, Western Carolina University, Cullowhee, NC 28723, USA. Electronic address: jamiewallen@email.wcu.edu.
  • Zhang H; Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.
  • Weis C; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Cui W; Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.
  • Foster BM; Department of Chemistry & Physics, Western Carolina University, Cullowhee, NC 28723, USA.
  • Ho CMW; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
  • Hammel M; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Tainer JA; Department of Molecular and Cellular Oncology, MD Anderson Cancer Center, Houston, TX 77054, USA; Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Gross ML; Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.
  • Ellenberger T; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA. Electronic address: tome@biochem.wustl.edu.
Structure ; 25(1): 157-166, 2017 01 03.
Article en En | MEDLINE | ID: mdl-28052235
The physical organization of DNA enzymes at a replication fork enables efficient copying of two antiparallel DNA strands, yet dynamic protein interactions within the replication complex complicate replisome structural studies. We employed a combination of crystallographic, native mass spectrometry and small-angle X-ray scattering experiments to capture alternative structures of a model replication system encoded by bacteriophage T7. Two molecules of DNA polymerase bind the ring-shaped primase-helicase in a conserved orientation and provide structural insight into how the acidic C-terminal tail of the primase-helicase contacts the DNA polymerase to facilitate loading of the polymerase onto DNA. A third DNA polymerase binds the ring in an offset manner that may enable polymerase exchange during replication. Alternative polymerase binding modes are also detected by small-angle X-ray scattering with DNA substrates present. Our collective results unveil complex motions within T7 replisome higher-order structures that are underpinned by multivalent protein-protein interactions with functional implications.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacteriófago T7 / ADN Primasa / ADN Polimerasa Dirigida por ADN Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacteriófago T7 / ADN Primasa / ADN Polimerasa Dirigida por ADN Idioma: En Revista: Structure Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos