L3MBTL1, a histone-methylation-dependent chromatin lock Journal Article


Authors: Trojer, P.; Li, G.; Sims, R. J. 3rd; Vaquero, A.; Kalakonda, N.; Boccuni, P.; Lee, D.; Erdjument-Bromage, H.; Tempst, P.; Nimer, S. D.; Wang, Y. H.; Reinberg, D.
Article Title: L3MBTL1, a histone-methylation-dependent chromatin lock
Abstract: Distinct histone lysine methylation marks are involved in transcriptional repression linked to the formation and maintenance of facultative heterochromatin, although the underlying mechanisms remain unclear. We demonstrate that the malignant-brain-tumor (MBT) protein L3MBTL1 is in a complex with core histones, histone H1b, HP1γ, and Rb. The MBT domain is structurally related to protein domains that directly bind methylated histone residues. Consistent with this, we found that the L3MBTL1 MBT domains compact nucleosomal arrays dependent on mono- and dimethylation of histone H4 lysine 20 and of histone H1b lysine 26. The MBT domains bind at least two nucleosomes simultaneously, linking repression of transcription to recognition of different histone marks by L3MBTL1. Consistently, L3MBTL1 was found to negatively regulate the expression of a subset of genes regulated by E2F, a factor that interacts with Rb. © 2007 Elsevier Inc. All rights reserved.
Keywords: controlled study; unclassified drug; human cell; methylation; protein domain; complex formation; gene expression; signaling; neoplasm proteins; cell line; protein binding; protein interaction; hela cells; dna; histone; chromatin; chromatin immunoprecipitation; histone h3; tumor protein; retinoblastoma protein; histones; nucleosome; nucleosomes; histone h4; heterochromatin protein 1; protein l3mbtl1; heterochromatin protein 1gamma; histone h1; histone h1b; e2f transcription factors
Journal Title: Cell
Volume: 129
Issue: 5
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2007-06-01
Start Page: 915
End Page: 928
Language: English
DOI: 10.1016/j.cell.2007.03.048
PUBMED: 17540172
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 106" - "Export Date: 17 November 2011" - "CODEN: CELLB" - "Source: Scopus"
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  1. Piernicola Boccuni
    16 Boccuni
  2. Paul J Tempst
    324 Tempst
  3. Stephen D Nimer
    347 Nimer