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Mass spectrometry of co-immunoprecipitation using Arabidopsis MKIP1-YFP as bait

ABSTRACT: Arabidopsis thaliana (Arabidopsis) MATURASE K INTERACTING PROTEIN1 (MKIP1) is a plastid-localized, non-canonical member of the starch-branching enzyme family. Here we used co-immunoprecipitation (IP) coupled with proteomics to identify proteins bound to MKIP1 in stably transformed Arabidopsis lines expressing MKIP1 fused to a C-terminal YFP tag in the wild-type (Col-0) background. Untransformed wild-type (Col-0) Arabidopsis plants served as control. Proteins co-precipitating with MKIP1-YFP were purified via anti-GFP beads and identified via shotgun proteomics. We performed three individual experiments each using multiple replicates. Each experiment was separately analysed using MaxQuant.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Rosette

SUBMITTER: Barbara Pfister

LAB HEAD: Samuel C. Zeeman

PROVIDER: PXD060108 | Pride | 2026-02-10

REPOSITORIES: Pride

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			Action	DRS
	20181022ma_11419_1_rep_2.raw	Raw
	20181022ma_11419_2_rep_2.raw	Raw
	20181022ma_11419_3_rep_2.raw	Raw
	20181022ma_11419_4.raw	Raw
	20181022ma_11419_7.raw	Raw

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