PER protein interactions and temperature compensation of a circadian clock in Drosophila

Science. 1995 Feb 24;267(5201):1169-72. doi: 10.1126/science.7855598.


The periods of circadian clocks are relatively temperature-insensitive. Indeed, the perL mutation in the Drosophila melanogaster period gene, a central component of the clock, affects temperature compensation as well as period length. The per protein (PER) contains a dimerization domain (PAS) within which the perL mutation is located. Amino acid substitutions at the perL position rendered PER dimerization temperature-sensitive. In addition, another region of PER interacted with PAS, and the perL mutation enhanced this putative intramolecular interaction, which may compete with PAS-PAS intermolecular interactions. Therefore, temperature compensation of circadian period in Drosophila may be due in part to temperature-independent PER activity, which is based on competition between inter- and intramolecular interactions with similar temperature coefficients.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Clocks*
  • Circadian Rhythm*
  • Drosophila Proteins
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / physiology*
  • Gene Expression Regulation
  • Genes, Insect
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Period Circadian Proteins
  • Point Mutation
  • Temperature


  • Drosophila Proteins
  • Nuclear Proteins
  • PER protein, Drosophila
  • Period Circadian Proteins