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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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DNA / chemistry
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Histones / chemistry*
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Histones / genetics
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Leucine Zippers
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Liver / ultrastructure*
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Macromolecular Substances
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Mice
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Molecular Sequence Data
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Nucleosomes / chemistry*
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Polymerase Chain Reaction
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Rats
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Sequence Homology, Nucleic Acid
Substances
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Histones
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Macromolecular Substances
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Nucleosomes
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DNA
Associated data
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GENBANK/M99065
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GENBANK/M99066