Single and combinatorial chromatin coupling events underlies the function of transcript factor Krüppel-like factor 11 in the regulation of gene networks

BMC Mol Biol. 2014 May 25:15:10. doi: 10.1186/1471-2199-15-10.

Abstract

Background: Krüppel-like factors (KLFs) are a group of master regulators of gene expression conserved from flies to human. However, scant information is available on either the mechanisms or functional impact of the coupling of KLF proteins to chromatin remodeling machines, a deterministic step in transcriptional regulation.

Results and discussion: In the current study, we use genome-wide analyses of chromatin immunoprecipitation (ChIP-on-Chip) and Affymetrix-based expression profiling to gain insight into how KLF11, a human transcription factor involved in tumor suppression and metabolic diseases, works by coupling to three co-factor groups: the Sin3-histone deacetylase system, WD40-domain containing proteins, and the HP1-histone methyltransferase system. Our results reveal that KLF11 regulates distinct gene networks involved in metabolism and growth by using single or combinatorial coupling events.

Conclusion: This study, the first of its type for any KLF protein, reveals that interactions with multiple chromatin systems are required for the full gene regulatory function of these proteins.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Apoptosis Regulatory Proteins
  • Cell Cycle Proteins / genetics*
  • Cells, Cultured
  • Chromatin / genetics*
  • Chromatin Assembly and Disassembly / genetics
  • Gene Expression Regulation / genetics
  • Gene Regulatory Networks / genetics*
  • Genome-Wide Association Study / methods
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / genetics
  • Humans
  • Repressor Proteins / genetics*
  • Transcription Factors / genetics*
  • Transcription, Genetic / genetics

Substances

  • Apoptosis Regulatory Proteins
  • Cell Cycle Proteins
  • Chromatin
  • KLF11 protein, human
  • Repressor Proteins
  • Transcription Factors
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase