Proteomics

Dataset Information

0

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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Publications

Rpd3/CoRest-mediated activity-dependent transcription regulates the flexibility in memory updating in Drosophila.

Takakura Mai M   Nakagawa Reiko R   Ota Takeshi T   Kimura Yoko Y   Ng Man Yung MY   Alia Abdalla G AG   Okuno Hiroyuki H   Hirano Yukinori Y  

Nature communications 20210127 1


Consolidated memory can be preserved or updated depending on the environmental change. Although such conflicting regulation may happen during memory updating, the flexibility of memory updating may have already been determined in the initial memory consolidation process. Here, we explored the gating mechanism for activity-dependent transcription in memory consolidation, which is unexpectedly linked to the later memory updating in Drosophila. Through proteomic analysis, we discovered that the com  ...[more]

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