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)
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
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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: |
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Communities: |
CSHL labs > Huang lab |
Depositing User: |
CSHL Librarian
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Date: |
1995 |
Date Deposited: |
10 Apr 2012 18:28 |
Last Modified: |
10 May 2013 19:10 |
Related URLs: |
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URI: |
https://repository.cshl.edu/id/eprint/25801 |
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