Proteomics

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Identification of the circadian ubiquitylated proteome of Drosophila melanogaster.


ABSTRACT: Circadian clocks have evolved as time-measuring molecular devices to help organisms adapt their physiology to daily changes in light and temperature. Cycling transcription has been long hypothesized to account for the wealth of rhythmic protein abundance. However, cyclic degradation signals such as ubiquitylation could shape the rhythmic protein landscape as well. In order to document the circadian ubiquitylated proteome of Drosophila melanogaster, we took advantage of a new means of Ub purification based on in vivo biotinylation of AviTag-tagged ubiquitin by the BirA protein, the bioUb system. NeutrAvidin-bound fractions of head lysates were collected at four circadian times six hours apart and proteins were identified and quantified using a proteomic-based approach.

INSTRUMENT(S): TripleTOF 4600

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Head

SUBMITTER: David Cornu  

LAB HEAD: David Cornu

PROVIDER: PXD005015 | Pride | 2018-05-22

REPOSITORIES: Pride

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