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  SAP18 promotes Krüppel-dependent transcriptional repression by enhancer-specific histone deacetylation.

Matyash, A., Singh, S., Hanes, S. D., Urlaub, H., & Jäckle, H. (2009). SAP18 promotes Krüppel-dependent transcriptional repression by enhancer-specific histone deacetylation. Journal of Biological Chemistry, 284(5), 3012-3020. doi:10.1074/jbc.M806163200.

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 Urheber:
Matyash, A.1, Autor           
Singh, S., Autor
Hanes, S. D., Autor
Urlaub, H.2, Autor           
Jäckle, H.1, Autor           
Affiliations:
1Department of Molecular Developmental Biology, MPI for biophysical chemistry, Max Planck Society, ou_578590              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Schlagwörter: Balo's concentric sclerosis; Childhood; Magnetic resonance spectroscopy; Diffusion tensor imaging; tNAA recovery
 Zusammenfassung: Body pattern formation during early embryogenesis of Drosophila melanogaster relies on a zygotic cascade of spatially restricted transcription factor activities. The gap gene Krüppel ranks at the top level of this cascade. It encodes a C2H2 zinc finger protein that interacts directly with cis-acting stripe enhancer elements of pair rule genes, such as even skipped and hairy, at the next level of the gene hierarchy. Krüppel mediates their transcriptional repression by direct association with the corepressor Drosophila C terminus-binding protein (dCtBP). However, for some Krüppel target genes, deletion of the dCtBP-binding sites does not abolish repression, implying a dCtBP-independent mode of repression. We identified Krüppel-binding proteins by mass spectrometry and found that SAP18 can both associate with Krüppel and support Krüppel-dependent repression. Genetic interaction studies combined with pharmacological and biochemical approaches suggest a site-specific mechanism of Krüppel-dependent gene silencing. The results suggest that Krüppel tethers the SAP18 bound histone deacetylase complex 1 at distinct enhancer elements, which causes repression via histone H3 deacetylation.

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Sprache(n): eng - English
 Datum: 2008-12-012009-01-30
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 412112
DOI: 10.1074/jbc.M806163200
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Titel: Journal of Biological Chemistry
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 284 (5) Artikelnummer: - Start- / Endseite: 3012 - 3020 Identifikator: -