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

Huang, Z. J., Curtin, K. D., Rosbash, M. (1995) PER protein interactions and temperature compensation of a circadian clock in Drosophila. Science, 267 (5201). pp. 1169-1172. ISSN 00368075 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/7855598

Abstract

The periods of circadian clocks are relatively temperature-insensitive. Indeed, the per(L) 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 per(L) mutation is located. Amino acid substitutions at the per(L) position rendered PER dimerization temperature-sensitive. In addition, another region of PER interacted with PAS, and the per(L) mutation enhanced this putative intramolecular interaction, which may compete with PAS-PAS intermolecular interactions. Therefore, 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 interaction with similar temperature coefficients.

Item Type: Paper
Uncontrolled Keywords: protein amino acid substitution article circadian rhythm controlled study dimerization drosophila melanogaster gene mutation nonhuman priority journal protein domain protein protein interaction temperature sensitivity Amino Acid Sequence Animal Biological Clocks Gene Expression Regulation Genes, Insect Molecular Sequence Data Nuclear Proteins Point Mutation Temperature
Subjects: organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > mutations
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
CSHL Authors:
Communities: CSHL labs > Huang lab
Depositing User: CSHL Librarian
Date Deposited: 10 Apr 2012 18:28
Last Modified: 10 May 2013 19:10
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25801

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