Negative regulation of the mouse aldolase A gene. A cell cycle-dependent DNA binding activity functions as a silencer of gene transcription

J Biol Chem. 1997 Dec 12;272(50):31641-7. doi: 10.1074/jbc.272.50.31641.

Abstract

The expression of aldolase A L-type mRNA is increased in growth-arrested mouse NIH3T3 cells and remarkably down-regulated in actively proliferating cells. Treatment of proliferating cells with cycloheximide abolished the down-regulation of L-type mRNA expression, thus indicating that a protein factor acts as repressor in proliferating cells. Transient transfection experiments in NIH3T3 cells showed that a negative regulatory cis-element (NRE) is involved in the modulation of the transcriptional activity of the distal L promoter. The repressor, which is a protein of approximately 97 kDa, binds the murine aldolase A NRE, revealing a much more intense DNA-protein complex in proliferating NIH3T3 cells than in serum-deprived cells. Mutations in the negative regulatory cis-element showed that the GA-rich motif is required for protein binding and silencer function. We conclude that the expression of L-type mRNA is modulated by the interaction between a cell cycle-dependent DNA-binding protein and the murine aldolase A NRE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Cycle
  • Cell Division
  • Cycloheximide / pharmacology
  • DNA / metabolism*
  • Dactinomycin / pharmacology
  • Fructose-Bisphosphate Aldolase / genetics*
  • Gene Expression Regulation, Enzymologic*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Nucleic Acid Synthesis Inhibitors / pharmacology
  • Promoter Regions, Genetic
  • Protein Synthesis Inhibitors / pharmacology
  • RNA, Messenger / metabolism
  • Ribonucleases / metabolism
  • Transcription, Genetic*

Substances

  • Nucleic Acid Synthesis Inhibitors
  • Protein Synthesis Inhibitors
  • RNA, Messenger
  • Dactinomycin
  • DNA
  • Cycloheximide
  • Ribonucleases
  • Fructose-Bisphosphate Aldolase