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Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.
Langelier, Marie-France; Steffen, Jamin D; Riccio, Amanda A; McCauley, Michael; Pascal, John M.
Afiliación
  • Langelier MF; Department of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boul. Edouard-Montpetit, Pavillon Roger-Gaudry, Montréal, QC, Canada, H3T 1J4.
  • Steffen JD; Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, 19107, USA.
  • Riccio AA; Department of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boul. Edouard-Montpetit, Pavillon Roger-Gaudry, Montréal, QC, Canada, H3T 1J4.
  • McCauley M; Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, 19107, USA.
  • Pascal JM; Department of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boul. Edouard-Montpetit, Pavillon Roger-Gaudry, Montréal, QC, Canada, H3T 1J4. john.pascal@umontreal.ca.
Methods Mol Biol ; 1608: 431-444, 2017.
Article en En | MEDLINE | ID: mdl-28695525
Human PARP-1, PARP-2, and PARP-3 are key players in the cellular response to DNA damage, during which their catalytic activities are acutely stimulated through interaction with DNA strand breaks. There are also roles for these PARPs outside of the DNA damage response, most notably for PARP-1 and PARP-2 in the regulation of gene expression. Here, we describe a general method to express and purify these DNA damage-dependent PARPs from E. coli cells for use in biochemical assays and for structural and functional analysis. The procedure allows for robust production of PARP enzymes that are free of contaminant DNA that can interfere with downstream analysis. The described protocols have been updated from our earlier reported methods, most importantly to introduce PARP inhibitors in the production scheme to cope with enzyme toxicity that can compromise the yield of purified protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Daño del ADN / Poli(ADP-Ribosa) Polimerasa-1 Límite: Animals / Humans Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Daño del ADN / Poli(ADP-Ribosa) Polimerasa-1 Límite: Animals / Humans Idioma: En Revista: Methods Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos