Methods for purification of proteins associated with cellular poly(ADP-Ribose) and pARP-Specific poly(ADP-Ribose)

Jennifer E. Rood, Anthony K.L. Leung, Paul Chang

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr. pADPr is synthesized by a family of enzymes called poly(ADP-ribose) polymerases (PARPs) that are themselves major targets of pADPr modification. Here, we outline two methods for the purification of pADPr-binding proteins via pADPr purification under native conditions: purification of cellular pADPr and pADPr covalently linked to specific PARPs. Together, these methods provide complementary approaches to the identification of noncovalent pADPr-protein interactions in the cell.

Original languageEnglish (US)
Title of host publicationPoly(ADP-ribose) Polymerase
Subtitle of host publicationMethods and Protocols
EditorsAlexei V. Tulin
Pages153-164
Number of pages12
DOIs
StatePublished - 2011
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume780
ISSN (Print)1064-3745

Keywords

  • Boronate affinity
  • Immunoprecipitation
  • PARP
  • Poly(ADP-ribose)
  • Poly(ADP-ribose) acceptor protein
  • Poly(ADP-ribose) associated protein
  • Poly(ADP-ribose) polymerase
  • Poly(ADP-ribose) purification
  • cis-diol

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Rood, J. E., Leung, A. K. L., & Chang, P. (2011). Methods for purification of proteins associated with cellular poly(ADP-Ribose) and pARP-Specific poly(ADP-Ribose). In A. V. Tulin (Ed.), Poly(ADP-ribose) Polymerase: Methods and Protocols (pp. 153-164). (Methods in Molecular Biology; Vol. 780). https://doi.org/10.1007/978-1-61779-270-0_10