Assembly of semihistone A24
- 1 January 1982
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 10 (18) , 5467-5481
- https://doi.org/10.1093/nar/10.18.5467
Abstract
Nucleosomal semihistone A24 (uH2A) is composed of histone H2A and ubiquitin peptides. The kinetics of incorporation of nascent H2A and ubiquitin into A24 of transformed chicken lymphocytes (MSB cells) have been examined by peptide mapping, COOH-terminus analysis, density labeling and isopycnic centrifugation of chromosomal proteins. We find that newly synthesized H2A is rapidly conjugated to ubiquitin. SDS-PAGE analysis of fractionated density gradients suggests, however, that newly synthesized ubiquitin becomes bound nonselectively to both new and preexisting H2A molecules.Keywords
This publication has 39 references indexed in Scilit:
- Nucleosome segregation at a defined mammalian chromosomal site.Proceedings of the National Academy of Sciences, 1982
- Chromosomal Proteins and Chromatin StructureAnnual Review of Biochemistry, 1975
- Hybrid troponin reconstituted from vertebrate and arthropod subunitsNature, 1975
- Two cell lines from lymphomas of Marek's disease.1974
- Isolation and partial characterization of an acid carboxypeptidase from yeastBiochemistry, 1974
- The dynamic state of liver nucleolar proteins as reflected by their changes during administration of thioacetamideLife Sciences, 1974
- Two-dimensional gel electrophoresis of acid-soluble nucleolar proteins of Walker 256 carcinosarcoma, regenerating liver, and thioacetamide-treated liver.1973
- Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins.1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The Significance of the “Partial Specific Volume” Obtained from Sedimentation Data*Biochemistry, 1966