Influence of thyroid hormone on ADP-ribosylation of nuclear proteins in cultured GH1 cells.
We present evidence that T3 can alter the ADP-ribosylation of chromatin associated proteins. Nuclei from GH1 cells were incubated with [adenylate-32P]NAD and the radioactivity incorporated into histone and non-histone proteins was quantitated and analyzed by gel electrophoresis and autoradiography. Incubation of GH1 cells for 24 h with T3 lowered by 40-70% the [32P]ADP-ribose incorporated into nuclear proteins. However, incubation for 3 h with T3 resulted in a stimulation instead of a decrease of in vitro [32P]ADP-ribose incorporation. The major ADP-ribosylated component electrophoresed as a 120,000 molecular mass non-histone protein, and radiolabeled histones were also observed. The same protein species were observed for all the experimental groups and T3 affected the extent of ADP-ribosylation but did not alter the sedimentation of the [32P]ADP-ribosylated components excised from chromatin after micrococcal nuclease digestion.
Aranda
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Instituto de Investigaciones Biomedicas, CSIC, Madrid, Spain.
Copp
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RP
Pascual
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Samuels
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HH
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism*; D010902:Pituitary Gland / Q000378:metabolism*; D051381:Rats; D013997:Time Factors; D014284:Triiodothyronine / Q000494:pharmacology*
D002843:Chromatin; D006609:High Mobility Group Proteins; D006657:Histones; D009687:Nuclear Proteins; D014284:Triiodothyronine; D000246:Adenosine Diphosphate Ribose