Open AccessMyristoylation profiling in human cells and zebrafish
Author(s) -
Malgorzata Broncel,
Remigiusz A. Serwa,
Paulina Ciepla,
Eberhard Krause,
Margaret J. Dallman,
Anthony I. Magee,
Edward W. Tate
Publication year - 2015
Publication title -
data in brief
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.122
H-Index - 30
ISSN - 2352-3409
DOI - 10.1016/j.dib.2015.06.010
Subject(s) - zebrafish , proteome , myristoylation , chemistry , hela , hek 293 cells , bioorthogonal chemistry , lipid anchored protein , proteomics , microbiology and biotechnology , biochemistry , biology , click chemistry , combinatorial chemistry , cell , apoptosis , phosphorylation , autophagy , gene
Human cells (HEK 293, HeLa, MCF-7) and zebrafish embryos were metabolically tagged with an alkynyl myristic acid probe, lysed with an SDS buffer and tagged proteomes ligated to multifunctional capture reagents via copper-catalyzed alkyne azide cycloaddition (CuAAC). This allowed for affinity enrichment and high-confidence identification, by delivering direct MS/MS evidence for the modification site, of 87 and 61 co-translationally myristoylated proteins in human cells and zebrafish, respectively. The data have been deposited to ProteomeXchange Consortium (Vizcaíno et al., 2014 Nat. Biotechnol., 32, 223-6) (PXD001863 and PXD001876) and are described in detail in Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic protein lipidation during vertebrate development׳ by Broncel et al., Angew. Chem. Int. Ed.
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