Publication Date:
1995-02-24
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Z J -- Curtin, K D -- Rosbash, M -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1169-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Brandeis University, Department of Biology, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855598" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
*Biological Clocks
;
*Circadian Rhythm
;
Drosophila Proteins
;
Drosophila melanogaster/genetics/*physiology
;
Gene Expression Regulation
;
Genes, Insect
;
Molecular Sequence Data
;
Nuclear Proteins/chemistry/genetics/*metabolism
;
Period Circadian Proteins
;
Point Mutation
;
Temperature
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
