Faculty Collaboration Database

Synthesis and ubiquitination of histones during myogenesis. Dev Biol 1987 Jan;119(1):85-93

Date

01/01/1987

Pubmed ID

3025034

DOI

10.1016/0012-1606(87)90209-0

Scopus ID

2-s2.0-0023103138 (requires institutional sign-in at Scopus site)   29 Citations

Abstract

One and two-dimensional polyacrylamide gel electrophoresis have revealed that cultures of postmitotic (G0) chicken skeletal myotube cells synthesize significant but reduced quantities of histone proteins as compared to their proliferating myoblast precursors. In addition, modulation of variant synthesis within the histone H2A and H3 classes may accompany myotube formation. That the histone bands contain no nonhistone contaminants was shown by exclusion of [3H]tryptophan. It is unlikely that these results reflect synthesis of histone by contaminating replicating cells, since a single treatment with cytosine arabinoside at the time of fusion effectively removed unfused cells while suppressing synthesis of DNA in the myotube cultures. The relatively sparse incorporation of label by major variants of the H2A class in dividing myoblasts was shown to be caused by heterogeneity due to phosphorylation and extensive ubiquitination, which decline at the time of myotube formation. As determined by quantitative Western-blotting, dividing myoblasts and myotubes contain an average of 1.0 and 0.4 molecules of ubiquitinated H2A (uH2A), respectively, per 10 nucleosomes.

Author List

Wunsch AM, Haas AL, Lough J

Author

John W. Lough PhD Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Animals
Cell Division
Cells, Cultured
Chick Embryo
Cytarabine
Electrophoresis, Polyacrylamide Gel
Histones
Muscles
Phosphorylation
Protein Processing, Post-Translational
Ubiquitins