Modification of nuclear matrix proteins by ADP‐ribosylation
- 1 December 1985
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 153 (2), 421-428
- https://doi.org/10.1111/j.1432-1033.1985.tb09319.x
Abstract
Nuclear matrices were isolated by treatment of isolated HeLa cell nuclei with high DNase I, pancreatic RNase and salt concentrations, ADP-ribosylated nuclear matrix proteins were identified by electrophoresis, blotting and autoradiography. In one experimental approach nuclear matrix proteins were labeled by exposure of permeabilized cells to the labeled precursor [32P]NAD. Alternatively, the cellular proteins were prelabeled with [35S]methionine and the ADP-ribosylated nuclear matrix proteins separated by aminophenyl boronate column chromatography. By both methods bands of modified proteins, though with differing intensities, were detected at 41, 43, 46, 51, 60, 64, 69, 73, 116, 140, 220 and 300 kDa. Approximately 2% of the total nuclear ADP-ribosyltransferase activity, but only 0.07% of the nuclear DNA, was tightly associated with the isolated nuclear matrix. The matrix-associated enzyme catalyzes the incorporation of [32P]ADP-ribose into acid-insoluble products of molecular mass 116 kDa and above, in a 3-aminobenzamide-inhibited, time-dependent reaction. The possible function of ADP-ribosylation of nuclear matrix proteins and of the attachment of ADP-ribosyltransferase to the nuclear matrix in the regulation of matrix-associated biochemical processes is discussed.This publication has 55 references indexed in Scilit:
- ADP-ribosylation of nonhistone proteins during the HeLa cell cycleBiochemical and Biophysical Research Communications, 1983
- Nuclear Matrix: A Cell‐Cycle‐Dependent Site of Increased Intranuclear Protein PhosphorylationEuropean Journal of Biochemistry, 1983
- Non-histone proteins and long-range organization of HeLa interphase DNAJournal of Molecular Biology, 1982
- Association of polyoma T antigen and DNA with the nuclear matrix from lytically infected 3T6 cellsCell, 1980
- Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cellsBiochemical and Biophysical Research Communications, 1979
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- ADP-ribosylation of nuclear protein A24Biochemical and Biophysical Research Communications, 1978
- Inhibition of rat liver Ca2+, Mg2+-dependent endonuclease activity by nicotinamide adenine dinucleotide and poly(adenosine diphosphate ribose) synthetaseBiochemical and Biophysical Research Communications, 1974
- Identification of poly(ADP-ribose) covalently bound to histone F1 in vivoBiochemical and Biophysical Research Communications, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970