MacroH2A, a Core Histone Containing a Large Nonhistone Region
- 4 September 1992
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 257 (5075), 1398-1400
- https://doi.org/10.1126/science.1529340
Abstract
A histone, macroH2A, nearly three times the size of conventional H2A histone, was found in rat liver nucleosomes. Its N-terminal third is 64 percent identical to a full-length mouse H2A. However, it also contains a large nonhistone region. This region has a segment that resembles a leucine zipper, a structure known to be involved in dimerization of some transcription factors. Nucleosomes containing macroH2A may have novel functions, possibly involving interactions with other nuclear proteins.Keywords
This publication has 32 references indexed in Scilit:
- X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled CoilScience, 1991
- Scissors-Grip Model for DNA Recognition by a Family of Leucine Zipper ProteinsScience, 1989
- Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding DomainsScience, 1989
- The role of the leucine zipper in the fos–jun interactionNature, 1988
- The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding ProteinsScience, 1988
- A conserved histone variant enriched in nucleoli of mammalian cellsCell, 1982
- Characterisation of Chromatin Fraction Bearing Pulse-Labelled RNA. 2. Quantification of Histones and high-Mobility-Group ProteinsEuropean Journal of Biochemistry, 1981
- Changes in chromatin folding in solutionJournal of Molecular Biology, 1980
- Fractionation of hen oviduct chromatin into transcriptionally active and inactive regions after selective micrococcal nuclease digestionCell, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970