Rearrangement of the histone H2A C-terminal domain in the nucleosome

Journal Article · Tue Jul 19 04:00:00 EDT 1994 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.91.15.6845· OSTI ID:86532

Usachenko, S I ^[1]; Bavykin, S G; Gavin, I M ^[2]; Bradbury, M ^[1]

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1. Univ. of California, Davis, CA (United States)
2. W.A. Engelhardt Institute of Molecular Biology of the Academy of Sciences, Vavilova (Russian Federation)

Using zero-length covalent protein-DNA crosslinking, the authors have mapped the histone-DNA contacts in nucleosome core particles from which the C- and N-terminal domains of histone H2A were selectively trimmed by trypsin or clostripain. They found that the flexible trypsin-sensitive C-terminal domain of histone H2A contacts the dyad axis, whereas its globular domain contacts the end of DNA in the nucleosome core particle. The appearance of the histone H2A contact at the dyad axis occurs only in the absence of linker DNA and does not depend on the absence of linker histones. The results show the ability of the histone H2A C-terminal domain to rearrange. This rearrangement might play a biological role in nucleosome disassembly and reassembly and the retention of the H2A-H2B dimer (or the whole octamer) during the passing of polymerases through the nucleosome.

• Sponsoring Organization: USDOE
• DOE Contract Number: FG03-88ER60673
• OSTI ID: 86532
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 15 Vol. 91; ISSN PNASA6; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
HISTONES
MOLECULAR STRUCTURE
NUCLEOSOMES