Affinity-based assays for the identification and quantitative evaluation of noncovalent poly(ADP-ribose)-binding proteins

Methods Mol Biol. 2011:780:93-115. doi: 10.1007/978-1-61779-270-0_7.

Abstract

Poly(ADP-ribose) polymerases have been linked to several cellular functions, most of which being mediated through the dynamics of poly(ADP-ribose) (pADPr). In several pathways, pADPr is the effector molecule that regulates cellular signaling and dictates biological outcomes. pAPDr is a central molecule that is capable of promoting both cell survival through the maintenance of genome integrity and cell death that occurs by way of a signal-mediated apoptotic-like process. Thus, interactions with pADPr are extremely important in bringing about the balanced regulation that controls cell fate. Further clues regarding these functions are emerging from a growing list of proteins with which pADPr interacts. Here, we describe the current approaches for investigating noncovalent protein interactions with pADPr.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Electrophoretic Mobility Shift Assay
  • Immunoprecipitation
  • Mass Spectrometry
  • Poly Adenosine Diphosphate Ribose / metabolism*
  • Poly(ADP-ribose) Polymerases / genetics
  • Poly(ADP-ribose) Polymerases / metabolism
  • Surface Plasmon Resonance

Substances

  • Carrier Proteins
  • Poly Adenosine Diphosphate Ribose
  • Poly(ADP-ribose) Polymerases