Proteomics

Dataset Information

CoRest’s acetylation acts as a temporal gate for activity-dependent transcription, limiting behavioral flexibility in Drosophila

ABSTRACT: In this project, to identify the proteins interacting with Rpd3 in the Drosophila mushroom body, the tandem affinity-purification(TAP) was performed. After in-solution digestion, the purified protein complex was analyzed by LC-MS/MS analysis using Orbitrap velos pro. PTM analysis was also performed to determine the acetylation site of CoRest, the Rpd3 interacting protein, purified from mushroom body.

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Yukinori Hirano 

PROVIDER: PXD021294 | JPOST Repository | Mon Dec 07 00:00:00 GMT 2020

REPOSITORIES: jPOST

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SN170725_Rpd3_TRPA1%20heat%20shock(-).mgf Mgf
SN170725_Rpd3_TRPA1%20heat%20shock(-).mzid Mzid
SN170725_Rpd3_TRPA1%20heat%20shock(-).raw Raw
SN170726_Rpd3_TRPA1%20heat%20shock%201h.mgf Mgf
SN170726_Rpd3_TRPA1%20heat%20shock%201h.raw Raw
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