On the presence of two new high mobility group‐like proteins in HeLa S3 cells
- 21 February 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 152 (2), 163-167
- https://doi.org/10.1016/0014-5793(83)80370-6
Abstract
Two phosphorylated HMG-like proteins with Mr approximately 10 000 have been isolated from HeLa S3 cells, one being present in metaphase and one in interphase cells. The amino acid compositions of these proteins are very similar but differ from the known HMG proteins. However, they exhibit similarities being rich in proline, basic and acidic amino acids. A possible role in chromatin condensation of the HMG-like protein characteristic for metaphase cells is suggested.Keywords
This publication has 19 references indexed in Scilit:
- HMG 17 in metaphase‐arrested and interphase HeLa S3 cellsFEBS Letters, 1981
- High mobility group proteins from CHO cells and their modifications during cell cycleBiochemical and Biophysical Research Communications, 1981
- Structure of transcriptionally active and inactive nucleosomes from butyrate-treated and control HeLa cellsBiochemistry, 1981
- On the presence of poly(ADP‐ribose) polymerase activity in metaphase chromosomes from HeLa S3 cellsFEBS Letters, 1980
- Post-synthetic modifications of nuclear proteins high mobility group proteins are methylatedBiochemical and Biophysical Research Communications, 1979
- The primary structure of the nucleosome‐associated chromosomal protein HMG 14FEBS Letters, 1979
- Nuclear protein modification and chromatin substructure. 1. Differential poly(adenosine diphosphate) ribosylation of chromosomal proteins in nuclei versus isolated nucleosomesBiochemistry, 1978
- Histone Phosphorylation and Chromatin Structure during Mitosis in Chinese Hamster CellsEuropean Journal of Biochemistry, 1978
- Chromosomal Subunits in Active Genes Have an Altered ConformationScience, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970