Increased PARP-1 levels in nuclear matrix isolated from heat shock treated rat liver |
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Authors: | G Zaalishvili E Zaldastanishvili M Karapetian T Zaalishvili |
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Institution: | Department of Genome Structure and Function, Life Sciences Research Center, Tbilisi, Georgia. giozaal@gmail.com |
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Abstract: | Poly(ADP-ribose) polymerase-1 (PARP-1), a chromatin-associated enzyme that catalyzes the NAD+-dependent addition of ADP-ribose polymers onto a variety of nuclear proteins, has been shown to be associated with the nuclear
matrix. PARP-1 levels in the nuclear matrix vary depending on the matrix isolation method used. The nuclear matrix appears
to be the most thermosensitive nuclear structure during heat shock. Here we provide evidence for the extensive translocation
of PARP-1 from chromatin to the nuclear matrix during heat shock. This translocation is accompanied by inhibition of PARP
activity in the nucleus and elevation of PARP activity in the nuclear matrix. Our data suggest that thermal destabilization
of the nuclear matrix is less likely to contribute to the translocation of PARP-1 to the nuclear matrix. |
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