Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2001-9-10
pubmed:abstractText
The Drosophila double-time (dbt) gene, which encodes a protein similar to vertebrate epsilon and delta isoforms of casein kinase I, is essential for circadian rhythmicity because it regulates the phosphorylation and stability of period (per) protein. Here, the circadian phenotype of a short-period dbt mutant allele (dbt(S)) was examined. The circadian period of the dbt(S) locomotor activity rhythm varied little when tested at constant temperatures ranging from 20 to 29 degrees C. However, per(L);dbt(S) flies exhibited a lack of temperature compensation like that of the long-period mutant (per(L)) flies. Light-pulse phase-response curves were obtained for wild-type, the short-period (per(S)), and dbt(S) genotypes. For the per(S) and dbt(S) genotypes, phase changes were larger than those for wild-type flies, the transition period from delays to advances was shorter, and the light-insensitive period was shorter. Immunohistochemical analysis of per protein levels demonstrated that per protein accumulates in photoreceptor nuclei later in dbt(S) than in wild-type and per(S) flies, and that it declines to lower levels in nuclei of dbt(S) flies than in nuclei of wild-type flies. Immunoblot analysis of per protein levels demonstrated that total per protein accumulation in dbt(S) heads is neither delayed nor reduced, whereas RNase protection analysis demonstrated that per mRNA accumulates later and declines sooner in dbt(S) heads than in wild-type heads. These results suggest that dbt can regulate the feedback of per protein on its mRNA by delaying the time at which it is translocated to nuclei and altering the level of nuclear PER during the declining phase of the cycle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7117-26
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11549722-Alleles, pubmed-meshheading:11549722-Animals, pubmed-meshheading:11549722-Behavior, Animal, pubmed-meshheading:11549722-Casein Kinase Iepsilon, pubmed-meshheading:11549722-Cell Nucleus, pubmed-meshheading:11549722-Circadian Rhythm, pubmed-meshheading:11549722-Darkness, pubmed-meshheading:11549722-Drosophila Proteins, pubmed-meshheading:11549722-Drosophila melanogaster, pubmed-meshheading:11549722-Feedback, pubmed-meshheading:11549722-Gene Expression Regulation, pubmed-meshheading:11549722-Immunohistochemistry, pubmed-meshheading:11549722-Light, pubmed-meshheading:11549722-Motor Activity, pubmed-meshheading:11549722-Mutation, pubmed-meshheading:11549722-Nuclear Proteins, pubmed-meshheading:11549722-Period Circadian Proteins, pubmed-meshheading:11549722-Periodicity, pubmed-meshheading:11549722-Phenotype, pubmed-meshheading:11549722-Photic Stimulation, pubmed-meshheading:11549722-Photoperiod, pubmed-meshheading:11549722-Photoreceptor Cells, Invertebrate, pubmed-meshheading:11549722-Protein Kinases, pubmed-meshheading:11549722-RNA, Messenger, pubmed-meshheading:11549722-Temperature
pubmed:year
2001
pubmed:articleTitle
The Drosophila double-timeS mutation delays the nuclear accumulation of period protein and affects the feedback regulation of period mRNA.
pubmed:affiliation
Department of Biology, West Virginia University, Morgantown, West Virginia 26506, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.