ADP-ribosylation of nonhistone proteins during the HeLa cell cycle

Min Kyung H Song; Kenneth W. Adolph

doi:10.1016/S0006-291X(83)80025-4

ADP-ribosylation of nonhistone proteins during the HeLa cell cycle

Min Kyung H Song, Kenneth W. Adolph

Biochemistry, Molecular Biology, and Biophysics (TMED)

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Abstract

ADP-ribosylation of nonhistone proteins during the HeLa cell cycle was investigated. Proteins were radiolabeled by incubating interphase nuclei and mitotic cells with the specific precursor, [³²P]NAD. Autoradiograms of two-dimensional gels of total nuclear nonhistone proteins showed a large number of modified species (more than 140). A complex pattern was also found for interphase chromatin. Nuclear scaffolds showed a simpler pattern of four major groups of modified species, which appeared to be the lamins and poly(ADP-ribose) polymerase. The labeling pattern for nonhistones of metaphase chromosomes was fundamentally different than with interphase nuclei. Autoradiograms were dominated by the incorporation of label into poly(ADP-ribose) polymerase.

Original language	English (US)
Pages (from-to)	938-945
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	115
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(83)80025-4
State	Published - Sep 30 1983

Bibliographical note

Funding Information:
This research was supported by grant GM 26440 from the National Institutes of Health and by funds from the Biomedical Research Support Grant of the University of Minnesota Medical School. We would like to thank Professor James W. Bodley for stimulating and useful discussions.

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abstract = "ADP-ribosylation of nonhistone proteins during the HeLa cell cycle was investigated. Proteins were radiolabeled by incubating interphase nuclei and mitotic cells with the specific precursor, [32P]NAD. Autoradiograms of two-dimensional gels of total nuclear nonhistone proteins showed a large number of modified species (more than 140). A complex pattern was also found for interphase chromatin. Nuclear scaffolds showed a simpler pattern of four major groups of modified species, which appeared to be the lamins and poly(ADP-ribose) polymerase. The labeling pattern for nonhistones of metaphase chromosomes was fundamentally different than with interphase nuclei. Autoradiograms were dominated by the incorporation of label into poly(ADP-ribose) polymerase.",

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AU - Adolph, Kenneth W.

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N2 - ADP-ribosylation of nonhistone proteins during the HeLa cell cycle was investigated. Proteins were radiolabeled by incubating interphase nuclei and mitotic cells with the specific precursor, [32P]NAD. Autoradiograms of two-dimensional gels of total nuclear nonhistone proteins showed a large number of modified species (more than 140). A complex pattern was also found for interphase chromatin. Nuclear scaffolds showed a simpler pattern of four major groups of modified species, which appeared to be the lamins and poly(ADP-ribose) polymerase. The labeling pattern for nonhistones of metaphase chromosomes was fundamentally different than with interphase nuclei. Autoradiograms were dominated by the incorporation of label into poly(ADP-ribose) polymerase.

AB - ADP-ribosylation of nonhistone proteins during the HeLa cell cycle was investigated. Proteins were radiolabeled by incubating interphase nuclei and mitotic cells with the specific precursor, [32P]NAD. Autoradiograms of two-dimensional gels of total nuclear nonhistone proteins showed a large number of modified species (more than 140). A complex pattern was also found for interphase chromatin. Nuclear scaffolds showed a simpler pattern of four major groups of modified species, which appeared to be the lamins and poly(ADP-ribose) polymerase. The labeling pattern for nonhistones of metaphase chromosomes was fundamentally different than with interphase nuclei. Autoradiograms were dominated by the incorporation of label into poly(ADP-ribose) polymerase.

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ADP-ribosylation of nonhistone proteins during the HeLa cell cycle

Abstract

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