Poly(ADP-Ribose) Biosynthesis

Detection and quantification of poly-ADP-ribosylated cellular proteins of spleen and liver tissues of mice in vivo by slot and Western blot immunoprobing using polyclonal antibody against mouse ADP-ribose polymer

“…The first task was to raise specific Ab against ADP-ribose polymer. It is known that PAR modification of proteins involves formation of a highly variable and heterogeneous polymer of ADP-ribose units on different proteins [1][2][3][4][5]. Thus, it was important to raise PAb against the heterogeneous mixture of naturally occurring ADP-ribose polymers, the Ag, to ensure that all types of PAR modified proteins could be detected.…”

“…Poly-ADP-ribosylation (PAR), a ubiquitous phenomenon in eukaryotes, refers to a reversible post-translational modification of cellular proteins [reviewed in [1][2][3][4][5]. PAR modifies target proteins enzymatically by adding successive ADP-ribose units from a donor, NAD + , in form of a branched or unbranched polymer.…”

“…The most preferred target proteins for PAR are nuclear or chromosomal proteins which include histones, endonuclease, topoisomerase I, DNA ligase II, PARP, etc. [2][3][4][6][7][8][9]. The polymer of ADP-ribose being charged causes alterations in the net charge and conformation of the target protein [3,10].…”

“…[2][3][4][6][7][8][9]. The polymer of ADP-ribose being charged causes alterations in the net charge and conformation of the target protein [3,10]. The altered charge and conformational states of modified chromosomal proteins, in turn, alter their interactions with DNA [3,[10][11][12][13].…”

“…The polymer of ADP-ribose being charged causes alterations in the net charge and conformation of the target protein [3,10]. The altered charge and conformational states of modified chromosomal proteins, in turn, alter their interactions with DNA [3,[10][11][12][13]. This alteration, thus, changes the conformational state of chromatin and affects its functional status [10,13].…”