TSH STIMULATES32P-LABELING OF THYROID NUCLEAR HMG 14, A PROTEIN ASSOCIATED WITH ACTIVELY TRANSCRIBED CHROMATIN
- 1 April 1982
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 110 (4) , 1459-1461
- https://doi.org/10.1210/endo-110-4-1459
Abstract
Thyroid slices were incubated with 32Pi with or without TSH. 32P-labeling of acid-soluble nuclear proteins was then examined by two-dimensional polyacrylamide gel electrophoresis and autoradiography. We found that TSH enhanced the labeling of the high mobility group protein HMG 14, a protein that is preferentially associated with actively transcribed chromatin. This observation suggests that changes in HMG 14 phosphorylation may be involved in mediating TSH-induced effects on the structure and. function of active chromatin.Keywords
This publication has 19 references indexed in Scilit:
- Nucleosome Cores Have Two Specific Binding Sites for Nonhistone Chromosomal Proteins HMG 14 and HMG 17Science, 1980
- Subunit structures of different electrophoretic forms of nucleosomes.Journal of Biological Chemistry, 1980
- Reconstitution of a deoxyribonuclease I-sensitive structure on active genes.Proceedings of the National Academy of Sciences, 1980
- The phosphorylation of high mobility group proteins 14 and 17 from Ehrlich ascites and L1210 invitroBiochemical and Biophysical Research Communications, 1980
- Influence of histone phosphorylation upon histone-histone interactions studied in vitroBiochemistry, 1980
- Interaction of HMG 14 and 17 with actively transcribed genesCell, 1980
- Phosphorylation of H1 and H5 histones by cyclic AMP-dependent protein kinase reduces DNA bindingBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1979
- Isolation of a subclass of nuclear proteins responsible for conferring a DNase I-sensitive structure on globin chromatin.Proceedings of the National Academy of Sciences, 1979
- Time Course of Thyrotropin-Dependent Protein Phosphorylation in Thyroid Slices*Endocrinology, 1978
- Studies on the Role and Mode of Operation of the Very‐Lysine‐Rich Histones in Eukaryote ChromatinEuropean Journal of Biochemistry, 1977