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Influence of thyroid hormone on ADP‐ribosylation of nuclear proteins in cultured GH1 cells
Author(s) -
Aranda Ana,
Copp Richard P.,
Pascual Angel,
Samuels Herbert H.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80143-q
Subject(s) - micrococcal nuclease , adp ribosylation , chromatin , histone , nad+ kinase , incubation , biochemistry , microbiology and biotechnology , biology , nuclear protein , adenylate kinase , histone h1 , enzyme , nucleosome , dna , gene , transcription factor
We present evidence that T3 can alter the ADP‐ribosylation of chromatin associated proteins. Nuclei from GH1 cells were incubated with [adenylate‐ 32 P]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 [ 32 P]ADP‐ribose incorporated into nuclear proteins. However, incubation for 3 h with T3 resulted in a simulation instead of a decrease of in vitro [ 32 P]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 [ 32 P]ADP‐ribosylated components excised from chromatin after micrococcal nuclease digestion.