The potato tuber mitochondrial proteome

Fernanda Salvato; Jesper F Havelund; Mingjie Chen; R Shyama Prasad Rao; Adelina Rogowska-Wrzesinska; Ole N Jensen; David R Gang; Jay J Thelen; Ian Max Møller

doi:10.1104/pp.113.229054

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The potato tuber mitochondrial proteome

Fernanda Salvato, Jesper F Havelund, Mingjie Chen, R Shyama Prasad Rao, Adelina Rogowska-Wrzesinska, Ole N Jensen, David R Gang, Jay J Thelen and Ian Max Møller

Plant physiology (Bethesda), Vol.164(2), pp.637-653

02/2014

DOI: https://doi.org/10.1104/pp.113.229054

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https://hdl.handle.net/2376/103433

PMID: 24351685

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Abstract

Fluorescence

Mitochondria - metabolism

Proteome - chemistry

Plant Tubers - metabolism

Subcellular Fractions - metabolism

Arabidopsis - metabolism

Protein Transport

Tobacco - cytology

Tandem Mass Spectrometry

Peptides - metabolism

Mitochondrial Proteins - metabolism

Plant Proteins - chemistry

Databases, Protein

Mitochondrial Proteins - chemistry

Chromatography, Liquid

Plant Epidermis - cytology

Solanum tuberosum - metabolism

Plant Proteins - metabolism

Protein Processing, Post-Translational

Proteome - metabolism

Mitochondria are called the powerhouses of the cell. To better understand the role of mitochondria in maintaining and regulating metabolism in storage tissues, highly purified mitochondria were isolated from dormant potato tubers (Solanum tuberosum 'Folva') and their proteome investigated. Proteins were resolved by one-dimensional gel electrophoresis, and tryptic peptides were extracted from gel slices and analyzed by liquid chromatography-tandem mass spectrometry using an Orbitrap XL. Using four different search programs, a total of 1,060 nonredundant proteins were identified in a quantitative manner using normalized spectral counts including as many as 5-fold more "extreme" proteins (low mass, high isoelectric point, hydrophobic) than previous mitochondrial proteome studies. We estimate that this compendium of proteins represents a high coverage of the potato tuber mitochondrial proteome (possibly as high as 85%). The dynamic range of protein expression spanned 1,800-fold and included nearly all components of the electron transport chain, tricarboxylic acid cycle, and protein import apparatus. Additionally, we identified 71 pentatricopeptide repeat proteins, 29 membrane carriers/transporters, a number of new proteins involved in coenzyme biosynthesis and iron metabolism, the pyruvate dehydrogenase kinase, and a type 2C protein phosphatase that may catalyze the dephosphorylation of the pyruvate dehydrogenase complex. Systematic analysis of prominent posttranslational modifications revealed that more than 50% of the identified proteins harbor at least one modification. The most prominently observed class of posttranslational modifications was oxidative modifications. This study reveals approximately 500 new or previously unconfirmed plant mitochondrial proteins and outlines a facile strategy for unbiased, near-comprehensive identification of mitochondrial proteins and their modified forms.

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Title: The potato tuber mitochondrial proteome
Creators: Fernanda Salvato - Department of Biochemistry and Interdisciplinary Plant Group, University of Missouri, Columbia, Missouri 65211
Jesper F Havelund
Mingjie Chen
R Shyama Prasad Rao
Adelina Rogowska-Wrzesinska
Ole N Jensen
David R Gang
Jay J Thelen
Ian Max Møller
Publication Details: Plant physiology (Bethesda), Vol.164(2), pp.637-653
Academic Unit: Biological Chemistry, Institute of
Publisher: United States
Identifiers: 99900546645301842
Language: English
Resource Type: Journal article