Abstract
Using heterochromatin-enriched fractions, we have detected specific binding of mononucleosomes to the N-terminal domain of the inner nuclear membrane protein lamin B receptor. Mass spectrometric analysis reveals that LBR-associated particles contain complex patterns of methylated/acetylated histones and are devoid of "euchromatic" epigenetic marks. LBR binds heterochromatin as a higher oligomer and forms distinct nuclear envelope microdomains in vivo. The organization of these membrane assemblies is affected significantly in heterozygous ic (ichthyosis) mutants, resulting in a variety of structural abnormalities and nuclear defects.
Original language | English |
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Pages (from-to) | 25567-73 |
Number of pages | 7 |
Journal | Journal of Biological Chemistry |
Volume | 279 |
Issue number | 24 |
DOIs | |
Publication status | Published - Jun 11 2004 |
Keywords
- Animals
- HeLa Cells
- Heterochromatin
- Humans
- Mass Spectrometry
- Nuclear Envelope
- Receptors, Cytoplasmic and Nuclear
- Journal Article
- Research Support, Non-U.S. Gov't
- Research Support, U.S. Gov't, P.H.S.