期刊
FEBS LETTERS
卷 584, 期 14, 页码 2999-3004出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.05.032
关键词
Chromatin; Histone methylation; Lamins; Premature senescence; Protein interaction
资金
- Centre National de la Recherche Scientifique (C.N.R.S.)
- Institut National de la Sante et de la Recherche Medicale (I.N.S.E.R.M.)
- Association Francaise de Lutte contre les Myopathies (A.F.M.)
- National Institutes of Health [AG025240]
- Plateforme d'ingenierie des proteines, service d'interactions des biomolecules, Institut de biologie integrative, Universite Pierre et Marie Curie, Paris 6 [IFR83]
Mutations in the lamin A/C (LMNA) gene that cause Hutchinson-Gilford progeria syndrome (HGPS) lead to expression of a protein called progerin with 50 amino acids deleted from the tail of prelamin A. In cells from patients with HGPS, both the amount and distribution of heterochromatin are altered. We designed in vitro assays to ask whether such alterations might reflect changes in chromatin, DNA and/or histone binding properties of progerin compared to wild-type lamin C-terminal tails. We show that progerin tail has a reduced DNA/chromatin binding capacity and modified trimethylated H3K27 binding pattern, offering a molecular mechanism for heterochromatin alterations related to HGPS. Structured summary: MINT-7893924, MINT-7893941, MINT-7893990, MINT-7894005, MINT-7894023, MINT-7894038:H3 (uniprotkb:Q71DI3) binds (MI:0407) to LaminA (uniprotkb:P02545) by surface plasmon resonance (MI:0107) MINT-7893957, MINT-7893974, MINT-7894055:H3 (uniprotkb:Q71DI3) binds (MI:0407) to progerin (uniprotkb: Q6UYC3) by surface plasmon resonance (MI:0107) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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