Proteomics

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AP-MS of tissue-specific protein complexes in C. elegans

ABSTRACT: We present a method for the tissue-specific purification of protein complexes from the nematode C. elegans, based on cell-type specific biotinylation. To purify proteins from specific C. elegans tissues, we adapted a system based on in vivo biotinylation of a protein of interest. In this approach, a protein of interest is tagged with the 15 amino acid Avi-tag, which can be biotinylated in vivo by the BirA biotin ligase from Escherichia coli. The biotinylated bait protein and any associated proteins are then purified with streptavidin-coated beads, and their identities are determined by mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Teck Yew Low  

LAB HEAD: Albert J.R. Heck

PROVIDER: PXD002139 | Pride | 2016-07-18

REPOSITORIES: Pride

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OR9_20140507_SSG_Selma_SeamCell_1control.pep.xml Pepxml
OR9_20140507_SSG_Selma_SeamCell_1control_12D.msf Msf
OR9_20140507_SSG_Selma_SeamCell_1control_12D.raw Raw
OR9_20140507_SSG_Selma_SeamCell_1control_13B.msf Msf
OR9_20140507_SSG_Selma_SeamCell_1control_13B.raw Raw
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Publications

<h4>Background</h4>Affinity purification followed by mass spectrometry (AP/MS) is a widely used approach to identify protein interactions and complexes. In multicellular organisms, the accurate identification of protein complexes by AP/MS is complicated by the potential heterogeneity of complexes in different tissues. Here, we present an in vivo biotinylation-based approach for the tissue-specific purification of protein complexes from Caenorhabditis elegans. Tissue-specific biotinylation is ach  ...[more]

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