Analysis of protein complexes in Arabidopsis leaves using size exclusion chromatography and label-free protein correlation profiling

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Title

Article ID

Volume

Year

Page Start

Issue

Type

86275

2017

research_article

PubSource

TAIR Reference ID

# 3704 Journal of proteomics

501776000

Scanned Date

Scanned By

Is Local Hard

Is Downloaded

Is Scanned

Melanie Trull

Ref Text

Is Peer Reviewed

IsPrintRef

IsE-Ref

Link

Doi

https://pubsearch.arabidopsis.org/pdfs/86275.pdf

http://doi.org/10.1016/j.jprot.2017.06.004

Authors

Aryal, U. K., McBride, Z., Chen, D., Xie, J., Szymanski, D. B.

Abstract

Protein complexes are fundamentally important for diverse cellular functions, and create functionalities that could never be achieved by a single polypeptide. Knowledge of the protein complex assemblies that exist in plant cells are limited. To close this gap, we applied an integrative proteomic approach that combines cell fractionation, protein chromatography and quantitative mass spectrometry (MS) to analyze the oligomerization state of thousands of proteins in a single experiment. Soluble extracts from intact Arabidopsis leaves were fractionated using size exclusion chromatography (SEC), and abundance profiles across the column fractions were quantified using label-free precursor ion (MS1) intensity. In duplicate experiments, we reproducibly detected 1693 proteins, of which 983 proteins were cytosolic. Based on the SEC profiles, approximately one third of all of the soluble proteins were predicted to be oligomeric. Our dataset includes both subunits of previously known complexes as well as hundreds of new protein complexes. The label-free MS1-based quantification method described here produced a highly useful dataset for the plant biology community, and provided a foundation to incorporate orthogonal protein complex separation methods so the composition and dynamics of protein complexes can be analyzed based on LC/MS profile data alone.

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28627464

1740779

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gene ATCG00490.1
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gene AT5G64460.8
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