A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16

Edwin R. Smith, Christelle Cayrou, Rong Huang, William S. Lane, Jacques Côté, John C. Lucchesi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

236 Scopus citations

Abstract

We describe a stable, multisubunit human histone acetyltransferase complex (hMSL) that contains homologs of the Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3. This complex shows strong specificity for histone H4 lysine 16 in chromatin in vitro, and RNA interference-mediated knockdown experiments reveal that it is responsible for the majority of H4 acetylation at lysine 16 in the cell. We also find that hMOF is a component of additional complexes, forming associations with host cell factor 1 and a protein distantly related to MSU (hMSL1v1). We find two versions of hMSL3 in the hMSL complex that differ by the presence of the chromodomain. Lastly, we find that reduction in the levels of hMSLs and acetylation of H4 at lysine 16 are correlated with reduced transcription of some genes and with a G2/M cell cycle arrest. This is of particular interest given the recent correlation of global loss of acetylation of lysine 16 in histone H4 with tumorigenesis.

Original languageEnglish (US)
Pages (from-to)9175-9188
Number of pages14
JournalMolecular and cellular biology
Volume25
Issue number21
DOIs
StatePublished - Nov 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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