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Mass spectrometry analysis of cleaved Ycf1p in the monomeric and dimeric states

ABSTRACT: Purified Ycf1p with a C-terminal 3xFLAG tag was obtained from a strain of yeast containing the Pep4p protease. The purified sample was subjected to blue native PAGE. Two gel bands, corresponding to monomeric and dimeric Pep4p-cleaved Ycf1p, were subjected to trypsin digestion.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Voula Kanelis

LAB HEAD: Voula Kanelis

PROVIDER: PXD057187 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20211028_Lumos_BickersS_Dimer.raw	Raw
	20211028_Lumos_BickersS_LFQ_Results.mgf	Mgf
	20211028_Lumos_BickersS_Mono.raw	Raw
	BickersS_YCF1_Modified_uniprot_UP000002311_Saccharomyces_cerevisiae_28092021.fasta	Fasta
	SarahBickersOctober282021-ScaffoldResults.mzid.gz_20211028_Lumos_BickersS_LFQ_Results__20211028_Lumos_BickersS_Dimer.MGF	Mzid

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Publications

Structure of a dimeric full-length ABC transporter.

Bickers Sarah C SC Benlekbir Samir S Rubinstein John L JL Kanelis Voula V

Nature communications 20241116 1

Activities of ATP binding cassette (ABC) proteins are regulated by multiple mechanisms, including protein interactions, phosphorylation, proteolytic processing, and/or oligomerization of the ABC protein itself. Here we present the structure of yeast cadmium factor 1 (Ycf1p) in its mature form following cleavage by Pep4p protease. Ycf1p, a C subfamily ABC protein (ABCC), is homologue of human multidrug resistance protein 1. Remarkably, a portion of cleaved Ycf1p forms a well-ordered dimer, alongs ...[more]

PMID: 39550367

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