TY - JOUR

T1 - The mitochondrial complexome of Arabidopsis thaliana

AU - Senkler, Jennifer

AU - Senkler, Michael

AU - Eubel, Holger

AU - Hildebrandt, Tatjana

AU - Lengwenus, Christian

AU - Schertl, Peter

AU - Schwarzländer, Markus

AU - Wagner, Stephan

AU - Wittig, Ilka

AU - Braun, Hans Peter

N1 - Funding information: This work was supported by the Deutsche Forschungsgemeinschaft (grant EU54/4-1 to HE, grant SCHW1719/1-1 to MS, grant SFB815/Z1 to IW and grant BR1829/10-2 to HPB).

PY - 2017/3/4

Y1 - 2017/3/4

N2 - Mitochondria are central to cellular metabolism and energy conversion. In plants they also enable photosynthesis through additional components and functional flexibility. A majority of those processes relies on the assembly of individual proteins to larger protein complexes, some of which operate as large molecular machines. There has been a strong interest in the makeup and function of mitochondrial protein complexes and protein–protein interactions in plants, but the experimental approaches used typically suffer from selectivity or bias. Here, we present a complexome profiling analysis for leaf mitochondria of the model plant Arabidopsis thaliana for the systematic characterization of protein assemblies. Purified organelle extracts were separated by 1D Blue native (BN) PAGE, a resulting gel lane was dissected into 70 slices (complexome fractions) and proteins in each slice were identified by label free quantitative shot-gun proteomics. Overall, 1359 unique proteins were identified, which were, on average, present in 17 complexome fractions each. Quantitative profiles of proteins along the BN gel lane were aligned by similarity, allowing us to visualize protein assemblies. The data allow re-annotating the subunit compositions of OXPHOS complexes, identifying assembly intermediates of OXPHOS complexes and assemblies of alternative respiratory oxidoreductases. Several protein complexes were discovered that have not yet been reported in plants, such as a 530 kDa Tat complex, 460 and 1000 kDa SAM complexes, a calcium ion uniporter complex (150 kDa) and several PPR protein complexes. We have set up a tailored online resource (https://complexomemap.de/at_mito_leaves) to deposit the data and to allow straightforward access and custom data analyses.

AB - Mitochondria are central to cellular metabolism and energy conversion. In plants they also enable photosynthesis through additional components and functional flexibility. A majority of those processes relies on the assembly of individual proteins to larger protein complexes, some of which operate as large molecular machines. There has been a strong interest in the makeup and function of mitochondrial protein complexes and protein–protein interactions in plants, but the experimental approaches used typically suffer from selectivity or bias. Here, we present a complexome profiling analysis for leaf mitochondria of the model plant Arabidopsis thaliana for the systematic characterization of protein assemblies. Purified organelle extracts were separated by 1D Blue native (BN) PAGE, a resulting gel lane was dissected into 70 slices (complexome fractions) and proteins in each slice were identified by label free quantitative shot-gun proteomics. Overall, 1359 unique proteins were identified, which were, on average, present in 17 complexome fractions each. Quantitative profiles of proteins along the BN gel lane were aligned by similarity, allowing us to visualize protein assemblies. The data allow re-annotating the subunit compositions of OXPHOS complexes, identifying assembly intermediates of OXPHOS complexes and assemblies of alternative respiratory oxidoreductases. Several protein complexes were discovered that have not yet been reported in plants, such as a 530 kDa Tat complex, 460 and 1000 kDa SAM complexes, a calcium ion uniporter complex (150 kDa) and several PPR protein complexes. We have set up a tailored online resource (https://complexomemap.de/at_mito_leaves) to deposit the data and to allow straightforward access and custom data analyses.

KW - alternative electron transport

KW - Arabidopsis thaliana

KW - complex I

KW - mitochondrial calcium uniporter

KW - mitochondrial metabolism

KW - PPR proteins

KW - proteomics

KW - respiratory chain

UR - http://www.scopus.com/inward/record.url?scp=85011429878&partnerID=8YFLogxK

U2 - 10.1111/tpj.13448

DO - 10.1111/tpj.13448

M3 - Article

C2 - 27943495

AN - SCOPUS:85011429878

VL - 89

SP - 1079

EP - 1092

JO - Plant Journal

JF - Plant Journal

SN - 0960-7412

IS - 6

ER -