The characterisation of 1SF monomer nucleosomes from hen oviduct and the partial characterisation of a third HMG14/17-like in such nucleosomes.
AUTOR(ES)
Goodwin, G H
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=326891Documentos Relacionados
- The interaction of high mobility proteins HMG14 and 17 with nucleosomes.
- Histone H1 and HMG 14/17 are deposited nonrandomly in the nucleus.
- HMG 14/17 binding affinities and DNAase I sensitivities of nucleoprotein particles.
- Properties of active nucleosomes as revealed by HMG 14 and 17 chromatography.
- Partial inhibition of histone deacetylase in active chromatin by HMG 14 and HMG 17.
