Automodification of PARP-1 mediates its tight binding to the nuclear matrix.
Poly(ADP-ribose) polymerase-1 (PARP-1), a nuclear enzyme that catalyzes the NAD(+)-dependent addition of ADP-ribose polymers on a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. As yet, the properties and conditions of this association are unclear. Here, we show the existence of two PARP-1 pools associated with the nuclear matrix of rat liver and the ability of PARP-1 automodification to facilitate its binding to the nuclear matrix.
Zaalishvili
Giorgi
G
Department of Functional Genomics, Institute of Molecular Biology and Biological Physics, Tbilisi 0160, Georgia. giozaal@gmail.com
Margiani
Dina
D
Kutalia
Ketevan
K
Suladze
Saba
S
Zaalishvili
Tengiz
T
D000818:Animals; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D015530:Nuclear Matrix / Q000201:enzymology*; D000071137:Poly (ADP-Ribose) Polymerase-1; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D051381:Rats; D017208:Rats, Wistar
C499322:Parp1 protein, rat; D000071137:Poly (ADP-Ribose) Polymerase-1; D011065:Poly(ADP-ribose) Polymerases