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 |
|---|---|
| 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 |
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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.
Cite this
The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope. / Makatsori, Dimitra; Kourmouli, Niki; Polioudaki, Hara; Shultz, Leonard D; McLean, Kelvin; Theodoropoulos, Panayiotis A; Singh, Prim B; Georgatos, Spyros D.
In: Journal of Biological Chemistry, Vol. 279, No. 24, 11.06.2004, p. 25567-73.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope
AU - Makatsori, Dimitra
AU - Kourmouli, Niki
AU - Polioudaki, Hara
AU - Shultz, Leonard D
AU - McLean, Kelvin
AU - Theodoropoulos, Panayiotis A
AU - Singh, Prim B
AU - Georgatos, Spyros D
PY - 2004/6/11
Y1 - 2004/6/11
N2 - 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.
AB - 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.
KW - Animals
KW - HeLa Cells
KW - Heterochromatin
KW - Humans
KW - Mass Spectrometry
KW - Nuclear Envelope
KW - Receptors, Cytoplasmic and Nuclear
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
KW - Research Support, U.S. Gov't, P.H.S.
U2 - 10.1074/jbc.M313606200
DO - 10.1074/jbc.M313606200
M3 - Article
VL - 279
SP - 25567
EP - 25573
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 24
ER -