Title:Poly(ADP-ribose): Structure, Physicochemical Properties and Quantification In Vivo, with Special Reference to Poly(ADP-ribose) Binding Protein Modules
Volume: 17
Issue: 7
Author(s): Masanao Miwa, Chieri Ida, Sachiko Yamashita, Masakazu Tanaka and Junichi Fujisawa
Affiliation:
Keywords:
Poly(ADP-ribose) binding modules, chain length, branching, poly(ADP-ribose) polymerases, poly(ADP-ribose)
glycohydrolase.
Abstract: PolyADP-ribosylation is a unique posttranslational modification of proteins, involved in
various cellular functions including stability of chromatin. PolyADP-ribosylation modifies acceptor
proteins with a large negatively charged poly(ADP-ribose) (PAR) to greatly change the structure and
function of the acceptor proteins. In addition various specific motifs of proteins were recently found to
interact non-covalently with PAR thereby changing the spaciotemporal activity of protein-protein interaction
in cells. However, the structure of PAR to which specific protein motifs should bind is not fully characterized.
The present work will review the structure, physicochemical properties and quantification of PAR in vivo, with special
reference to PAR binding protein modules.
