Identification of factors mediating the developmental regulation of the early acting -3.9 kb chicken lysozyme enhancer element

Nucleic Acids Res. 2001 Nov 15;29(22):4551-60. doi: 10.1093/nar/29.22.4551.

Abstract

The chicken lysozyme gene -3.9 kb enhancer forms a DNase I hypersensitive site (DHS) early in macrophage differentiation, but not in more primitive multipotent myeloid precursor cells. A nucleosome becomes precisely positioned across the enhancer in parallel with DHS formation. In transfection assays, the 5'-part of the -3.9 kb element has ubiquitous enhancer activity. The 3'-part has no stimulatory activity, but is necessary for enhancer repression in lysozyme non-expressing cells. Recent studies have shown that the chromatin fine structure of this region is affected by inhibition of histone deacetylase activity after Trichostatin A (TSA) treatment, but only in lysozyme non-expressing cells. These results indicated a developmental modification of chromatin structure from a dynamic, but inactive, to a stabilised, possibly hyperacetylated, active state. Here we have identified positively and negatively acting transcription factors binding to the -3.9 kb enhancer and determined their contribution to enhancer activity. Furthermore, we examined the influence of TSA treatment on enhancer activity in macrophage cells and lysozyme non-expressing cells, including multipotent macrophage precursors. Interestingly, TSA treatment was able to restore enhancer activity fully in macrophage precursor cells, but not in non-macrophage lineage cells. These results suggest (i) that the transcription factor complement of multipotent progenitor cells is similar to that of lysozyme-expressing cells and (ii) that developmental regulation of the -3.9 kb enhancer is mediated by the interplay of repressing and activating factors that respond to or initiate changes in the chromatin acetylation state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AT Rich Sequence / genetics
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism
  • Animals
  • Base Sequence
  • Binding Sites / genetics
  • Binding, Competitive
  • Cell Differentiation / genetics
  • Cell Line, Transformed
  • DNA / genetics
  • DNA / metabolism*
  • DNA Footprinting
  • Electrophoretic Mobility Shift Assay
  • Enhancer Elements, Genetic / genetics*
  • Gene Expression Regulation, Developmental / drug effects
  • Hematopoiesis / genetics
  • Histone Acetyltransferases
  • Hydroxamic Acids / pharmacology
  • Luciferases / genetics
  • Luciferases / metabolism
  • Macrophages / cytology
  • Macrophages / drug effects
  • Macrophages / metabolism
  • Molecular Sequence Data
  • Muramidase / genetics*
  • Mutation
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Plasmids / genetics
  • Protein Binding
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Trans-Activators / genetics
  • Trans-Activators / metabolism
  • Transcription Factors / metabolism*
  • Transfection
  • beta-Galactosidase / genetics
  • beta-Galactosidase / metabolism

Substances

  • Hydroxamic Acids
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • trichostatin A
  • DNA
  • Luciferases
  • Acetyltransferases
  • Histone Acetyltransferases
  • Muramidase
  • beta-Galactosidase