The periods of circadian clocks are relatively temperature-insensitive
. Indeed, the per(L) mutation in the Drosophila melanogaster period ge
ne, a central component of the clock, affects temperature compensation
as well as period length. The per protein (PER) contains a dimerizati
on domain (PAS) within which the per(L) mutation is located. Amino aci
d substitutions at the per(L) position rendered PER dimerization tempe
rature-sensitive. In addition, another region of PER interacted with P
AS, and the per(L) mutation enhanced this putative intramolecular inte
raction, which may compete with PAS-PAS intermolecular interactions. T
herefore, temperature compensation of circadian period in Drosophila m
ay be due in part to temperature-independent PER activity, which is ba
sed on competition between inter- and intramolecular interactions with
similar temperature coefficients.