Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins
Kenneth W. Adolph
Molecular Biology (TMED)
Changes in ADP-ribosylation of nuclear proteins during the HeLa cell cycle were determined. Portions of synchronized cultures were withdrawn at intervals and cells were permeabilized by resuspension in hypotonic buffer containing detergents. Nuclear proteins were radioactively labeled by incubating samples with [32P]NAD. Modified species were resolved using one-dimensional and two-dimensional polyacrylamide gel electrophoresis. Measurements of the incorporation of [32P]NAD by permeabilized cells showed that ADP-ribosylation is a significant modification throughout the cell cycle. A twofold increase was detected during S phase. Autoradiograms of one-dimensional sodium dodecyl sulfate-polyacrylamide gels revealed that many nuclear nonhistones are modified, though the major acceptors of 32P were the histones and a 116,000-Da species (poly(ADP-ribose) polymerase). The same modified proteins were present through the cell cycle, but densitometry of autoradiograms demonstrated a general increase in the level of incorporation in S phase. Autoradiograms of two-dimensional gels of nuclear proteins labeled with [32P]NAD were consistent with these results. Although nonhistones of isolated metaphase chromosomes show a substantial reduction in ADP-ribosylation, histone modification is essentially unchanged in metaphase.
Archives of Biochemistry and Biophysics
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Nuclear Proteins Medicine & Life Sciences
NAD Medicine & Life Sciences
Adenosine Diphosphate Chemical Compounds
Cells Chemical Compounds
Cell Cycle Medicine & Life Sciences
Metaphase Medicine & Life Sciences
S Phase Medicine & Life Sciences
Histones Chemical Compounds
Adolph, K. W. (1985). Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins. Archives of Biochemistry and Biophysics, 243(2), 427-438. https://doi.org/10.1016/0003-9861(85)90519-3
Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins. / Adolph, Kenneth W.
In: Archives of Biochemistry and Biophysics, Vol. 243, No. 2, 12.1985, p. 427-438.
Adolph, KW 1985, 'Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins', Archives of Biochemistry and Biophysics, vol. 243, no. 2, pp. 427-438. https://doi.org/10.1016/0003-9861(85)90519-3
Adolph KW. Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins. Archives of Biochemistry and Biophysics. 1985 Dec;243(2):427-438. https://doi.org/10.1016/0003-9861(85)90519-3
Adolph, Kenneth W. / Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins. In: Archives of Biochemistry and Biophysics. 1985 ; Vol. 243, No. 2. pp. 427-438.
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title = "Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins",
abstract = "Changes in ADP-ribosylation of nuclear proteins during the HeLa cell cycle were determined. Portions of synchronized cultures were withdrawn at intervals and cells were permeabilized by resuspension in hypotonic buffer containing detergents. Nuclear proteins were radioactively labeled by incubating samples with [32P]NAD. Modified species were resolved using one-dimensional and two-dimensional polyacrylamide gel electrophoresis. Measurements of the incorporation of [32P]NAD by permeabilized cells showed that ADP-ribosylation is a significant modification throughout the cell cycle. A twofold increase was detected during S phase. Autoradiograms of one-dimensional sodium dodecyl sulfate-polyacrylamide gels revealed that many nuclear nonhistones are modified, though the major acceptors of 32P were the histones and a 116,000-Da species (poly(ADP-ribose) polymerase). The same modified proteins were present through the cell cycle, but densitometry of autoradiograms demonstrated a general increase in the level of incorporation in S phase. Autoradiograms of two-dimensional gels of nuclear proteins labeled with [32P]NAD were consistent with these results. Although nonhistones of isolated metaphase chromosomes show a substantial reduction in ADP-ribosylation, histone modification is essentially unchanged in metaphase.",
author = "Adolph, {Kenneth W.}",
journal = "Archives of Biochemistry and Biophysics",
T1 - Cell cycle variations in ADP-ribosylation of HeLa nuclear proteins
AU - Adolph, Kenneth W.
N2 - Changes in ADP-ribosylation of nuclear proteins during the HeLa cell cycle were determined. Portions of synchronized cultures were withdrawn at intervals and cells were permeabilized by resuspension in hypotonic buffer containing detergents. Nuclear proteins were radioactively labeled by incubating samples with [32P]NAD. Modified species were resolved using one-dimensional and two-dimensional polyacrylamide gel electrophoresis. Measurements of the incorporation of [32P]NAD by permeabilized cells showed that ADP-ribosylation is a significant modification throughout the cell cycle. A twofold increase was detected during S phase. Autoradiograms of one-dimensional sodium dodecyl sulfate-polyacrylamide gels revealed that many nuclear nonhistones are modified, though the major acceptors of 32P were the histones and a 116,000-Da species (poly(ADP-ribose) polymerase). The same modified proteins were present through the cell cycle, but densitometry of autoradiograms demonstrated a general increase in the level of incorporation in S phase. Autoradiograms of two-dimensional gels of nuclear proteins labeled with [32P]NAD were consistent with these results. Although nonhistones of isolated metaphase chromosomes show a substantial reduction in ADP-ribosylation, histone modification is essentially unchanged in metaphase.
AB - Changes in ADP-ribosylation of nuclear proteins during the HeLa cell cycle were determined. Portions of synchronized cultures were withdrawn at intervals and cells were permeabilized by resuspension in hypotonic buffer containing detergents. Nuclear proteins were radioactively labeled by incubating samples with [32P]NAD. Modified species were resolved using one-dimensional and two-dimensional polyacrylamide gel electrophoresis. Measurements of the incorporation of [32P]NAD by permeabilized cells showed that ADP-ribosylation is a significant modification throughout the cell cycle. A twofold increase was detected during S phase. Autoradiograms of one-dimensional sodium dodecyl sulfate-polyacrylamide gels revealed that many nuclear nonhistones are modified, though the major acceptors of 32P were the histones and a 116,000-Da species (poly(ADP-ribose) polymerase). The same modified proteins were present through the cell cycle, but densitometry of autoradiograms demonstrated a general increase in the level of incorporation in S phase. Autoradiograms of two-dimensional gels of nuclear proteins labeled with [32P]NAD were consistent with these results. Although nonhistones of isolated metaphase chromosomes show a substantial reduction in ADP-ribosylation, histone modification is essentially unchanged in metaphase.
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics