Proteomics

Dataset Information

0

Fatty-acyl conjugated amino-hexyl agarose pulldown with HeLa SILAC whole cell extract

ABSTRACT: C10:0 and C14:0 fatty acids were conjugated onto agarose beads, and used for pull-down with stable isotope (light: K0R0, heavy: K8R10) labeled Hela whole cell extract. C2:0 conjugated beads were used as control. Both forward (C2:0-light, C10:0 or C14:0-heavy) and reverse (C2:0-heavy, C10:0 or C14:0-light) labeling and pull-down experiments were performed.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: John Coan  

LAB HEAD: Katrin Chua

PROVIDER: PXD015272 | Pride | 2019-10-02

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
C10vsC2FWDlower.raw Raw
C10vsC2FWDupper.raw Raw
C10vsC2REVlower.raw Raw
C10vsC2REVupper.raw Raw
C10vsC2searches.7z Other
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Publications

Binding to medium and long chain fatty acyls is a common property of HEAT and ARM repeat modules.

Li Tie-Mei TM   Coan John P JP   Krajewski Krzysztof K   Zhang Lichao L   Elias Joshua E JE   Strahl Brian D BD   Gozani Or O   Chua Katrin F KF  

Scientific reports 20191002 1

Covalent post-translational modification (PTM) of proteins with acyl groups of various carbon chain-lengths regulates diverse biological processes ranging from chromatin dynamics to subcellular localization. While the YEATS domain has been found to be a prominent reader of acetylation and other short acyl modifications, whether additional acyl-lysine reader domains exist, particularly for longer carbon chains, is unclear. Here, we employed a quantitative proteomic approach using various modified  ...[more]