The active immunoglobulin κ chain gene is packaged by non-ubiquitin-conjugated nucleosomes

S. Y. Huang, M. B. Barnard, M. Xu, S. Matsui, S. M. Rose, W. T. Garrard

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

To elucidate the molecular features of active chromatin, we have mapped, by two-dimensional electrophoresis, the protein composition of nucleosomes that package the immunoglobulin κ chain gene of mouse plasmacytoma cells. Nucleoprotein particles that possess the active κ chain gene comigrate with bulk mononucleosomes that contain high mobility group proteins HMG-14 or -17 but lack histone H1. High electrophoretic resolution of the underlying core particles, after removal of ubiquitin by isopeptidase treatment, reveals that these nucleosomes are nonubiquitinated, even though they coincidently migrrate with bulk ubiquitinated particles. This distinctive electrophoretic behavior may be correlated with the presence of histone H2A.X. Nucleosomes exhibiting these unusual properties appear to span at least 10 kilobases, in both transcribed and nontranscribed regions, suggesting that mechanisms independent of transcription exist to initiate, maintain, and propagate a common chromatin phenotype over long distances along the κ chain locus.

Original languageEnglish (US)
Pages (from-to)3738-3742
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number11
DOIs
StatePublished - Jan 1 1986

ASJC Scopus subject areas

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