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Eur J Hum Genet. 2014 Sep;22(9):1117-23. doi: 10.1038/ejhg.2013.306. Epub 2014 Jan 22.

DNA polymorphism and epigenetic marks modulate the affinity of a scaffold/matrix attachment region to the nuclear matrix.

Author information

1
1] NN Blokhin Russian Cancer Research Center, RAMS, Moscow, Russia [2] UMR 8126, Université Paris Sud, CNRS, Institut de cancérologie Gustave Roussy, Villejuif, France.
2
1] UMR 8126, Université Paris Sud, CNRS, Institut de cancérologie Gustave Roussy, Villejuif, France [2] LIA 1066, Laboratoire Franco-Russe de recherche en oncologie, Villejuif, France [3] INSERM U1046, Montpellier, France.
3
NN Blokhin Russian Cancer Research Center, RAMS, Moscow, Russia.
4
1] UMR 8126, Université Paris Sud, CNRS, Institut de cancérologie Gustave Roussy, Villejuif, France [2] LIA 1066, Laboratoire Franco-Russe de recherche en oncologie, Villejuif, France.
5
Department of Human Genetics, Leiden University Medical Center, Leiden, The Netherlands.
6
INSERM U1046, Montpellier, France.
7
1] UMR 8126, Université Paris Sud, CNRS, Institut de cancérologie Gustave Roussy, Villejuif, France [2] LIA 1066, Laboratoire Franco-Russe de recherche en oncologie, Villejuif, France [3] NK Koltsov Institute of Developmental Biology, RAS, Moscow, Russia.

Abstract

Mechanisms that regulate attachment of the scaffold/matrix attachment regions (S/MARs) to the nuclear matrix remain largely unknown. We have studied the effect of simple sequence length polymorphism (SSLP), DNA methylation and chromatin organization in an S/MAR implicated in facioscapulohumeral dystrophy (FSHD), a hereditary disease linked to a partial deletion of the D4Z4 repeat array on chromosome 4q. This FSHD-related nuclear matrix attachment region (FR-MAR) loses its efficiency in myoblasts from FSHD patients. Three criteria were found to be important for high-affinity interaction between the FR-MAR and the nuclear matrix: the presence of a specific SSLP haplotype in chromosomal DNA, the methylation of one specific CpG within the FR-MAR and the absence of histone H3 acetylated on lysine 9 in the relevant chromatin fragment.

PMID:
24448543
PMCID:
PMC4135416
DOI:
10.1038/ejhg.2013.306
[Indexed for MEDLINE]
Free PMC Article

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