Variations in ADP-ribosylation of nuclear scaffold proteins during the Hela cell cycle

Kenneth W. Adolph; Min Kyung H Song

doi:10.1016/0006-291X(85)90261-X

Variations in ADP-ribosylation of nuclear scaffold proteins during the Hela cell cycle

Kenneth W. Adolph, Min Kyung H Song

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

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Abstract

Cell cycle variations in ADP-ribosylation of nuclear scaffold proteins were determined. Nuclei of synchronized cells were isolated and labeled with [³²P]NAD before nuclear scaffolds were obtained by digestion of DNA with DNase I and extraction of proteins with 2M NaCl. Autoradiograms revealed the three groups of "lamins" and a species identified as poly(ADP-ribose) polymerase to be the primary ADP-ribosylated proteins. The patterns of modification of nuclear scaffold proteins displayed similar features through the cell cycle. Radioactivity in the lamins increased from 20% in early-S phase to 40% in G1 phase of the next cell cycle.

Original language	English (US)
Pages (from-to)	840-847
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	126
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(85)90261-X
State	Published - Jan 31 1985

Bibliographical note

Funding Information:
This research was supported by funds from the Graduate School of the University of Minnesota, by funds from the Biomedical Research Support Grant the University of Minnesota Medical School, and by grant GM26440 from the National Institutes of Health.

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abstract = "Cell cycle variations in ADP-ribosylation of nuclear scaffold proteins were determined. Nuclei of synchronized cells were isolated and labeled with [32P]NAD before nuclear scaffolds were obtained by digestion of DNA with DNase I and extraction of proteins with 2M NaCl. Autoradiograms revealed the three groups of {"}lamins{"} and a species identified as poly(ADP-ribose) polymerase to be the primary ADP-ribosylated proteins. The patterns of modification of nuclear scaffold proteins displayed similar features through the cell cycle. Radioactivity in the lamins increased from 20% in early-S phase to 40% in G1 phase of the next cell cycle.",

author = "Adolph, {Kenneth W.} and Song, {Min Kyung H}",

note = "Funding Information: This research was supported by funds from the Graduate School of the University of Minnesota, by funds from the Biomedical Research Support Grant the University of Minnesota Medical School, and by grant GM26440 from the National Institutes of Health.",

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AU - Song, Min Kyung H

N1 - Funding Information: This research was supported by funds from the Graduate School of the University of Minnesota, by funds from the Biomedical Research Support Grant the University of Minnesota Medical School, and by grant GM26440 from the National Institutes of Health.

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N2 - Cell cycle variations in ADP-ribosylation of nuclear scaffold proteins were determined. Nuclei of synchronized cells were isolated and labeled with [32P]NAD before nuclear scaffolds were obtained by digestion of DNA with DNase I and extraction of proteins with 2M NaCl. Autoradiograms revealed the three groups of "lamins" and a species identified as poly(ADP-ribose) polymerase to be the primary ADP-ribosylated proteins. The patterns of modification of nuclear scaffold proteins displayed similar features through the cell cycle. Radioactivity in the lamins increased from 20% in early-S phase to 40% in G1 phase of the next cell cycle.

AB - Cell cycle variations in ADP-ribosylation of nuclear scaffold proteins were determined. Nuclei of synchronized cells were isolated and labeled with [32P]NAD before nuclear scaffolds were obtained by digestion of DNA with DNase I and extraction of proteins with 2M NaCl. Autoradiograms revealed the three groups of "lamins" and a species identified as poly(ADP-ribose) polymerase to be the primary ADP-ribosylated proteins. The patterns of modification of nuclear scaffold proteins displayed similar features through the cell cycle. Radioactivity in the lamins increased from 20% in early-S phase to 40% in G1 phase of the next cell cycle.

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Variations in ADP-ribosylation of nuclear scaffold proteins during the Hela cell cycle

Abstract

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