Open AccessRapid turnover of the histone-ubiquitin conjugate, protein A24
Author(s) -
Ronald L. Seale
Publication year - 1981
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/9.13.3151
Subject(s) - moiety , biology , ubiquitin , histone , protein turnover , conjugate , microbiology and biotechnology , biochemistry , biophysics , protein biosynthesis , stereochemistry , dna , chemistry , gene , mathematical analysis , mathematics
The specific activity of protein A24 was found to exceed that of the core histones by 2-3 fold following a brief labeling period. Accordingly, the A24 protein was found to be unstable, with a decay half-life of 90 minutes. When decay of the ubiquitin moiety was measured, it was found to turn over more extensively than the H2A moiety.
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