Open AccessThe characterisation of 1SF monomer nucleosomes from hen oviduct and the partial characterisation of a third HMG14/17-like protein in such nucleosomes
Author(s) -
Graham H. Goodwin,
Carol Wright,
Ernest W. Johns
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/9.12.2761
Subject(s) - biology , nucleosome , monomer , oviduct , microbiology and biotechnology , biophysics , biochemistry , histone , dna , materials science , polymer , composite material , endocrinology
Nucleosomes released from oviduct nuclei during brief micrococcal nuclease digestions are enriched in transcribed sequences (bloom K.S. and Anderson, J.N. (1978) Cell, 15, 141-150). Such nucleosomes released into this 1Sf supernatant fraction are enriched in proteins HMG14, 17 and a third lower molecular weight protein which we show in this paper to be related to HMG14 and 17. This protein, which we call HMGY, runs as a doublet on polyacrylamide gels. A similar doublet is present in smaller quantities in chicken erythrocyte nuclei. Monomer nucleosomes in the 1SF supernatant have been separated by polyacrylamide gel electrophoresis into two main bands. The slower moving band contains the three HMG proteins HMG14, 17 and Y but lacks histone H1.