Linked Life Data

7855598

Source:http://linkedlifedata.com/resource/pubmed/id/7855598

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5201
pubmed:dateCreated
1995-3-15
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1169-72
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
PER protein interactions and temperature compensation of a circadian clock in Drosophila.
pubmed:affiliation
Howard Hughes Medical Institute, Brandeis University, Department of Biology, Waltham, MA 02254.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.