Premium
A survey of the plant mitochondrial proteome in relation to development
Author(s) -
Bardel Juliette,
Louwagie Mathilde,
Jaquinod Michel,
Jourdain Agnès,
Luche Sylvie,
Rabilloud Thierry,
Macherel David,
Garin Jérôme,
Bourguig Jacques
Publication year - 2002
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200207)2:7<880::aid-prot880>3.0.co;2-0
Subject(s) - proteome , coomassie brilliant blue , proteomics , mitochondrion , biochemistry , biology , edman degradation , mass spectrometry , gel electrophoresis , polyacrylamide gel electrophoresis , two dimensional gel electrophoresis , tandem mass spectrometry , electrospray ionization , chemistry , chromatography , staining , peptide sequence , genetics , gene , enzyme
To expand the functional analysis of plant mitochondria, we have undertaken the building of the proteome of pea mitochondria purified from leaves (green and etiolated), roots and seeds. In the first stage, we focused our proteomic exploration on the soluble protein complement of the green leaf mitochondria. We used traditional two‐dimensional polyacrylamide gel electrophoresis, in combination with size exclusion chromatography as a third dimension, to identify the major proteins and further resolve their macromolecular complexity. The two‐dimensional map of soluble proteins of green leaf mitochondria revealed 433 spots (with Coomassie blue staining) and around 73% of the proteins (in mass) were identified using three different approaches: Edman degradation, matrix‐assisted laser desorption/ionization mass spectrometry and electrospray ionization tandem mass spectrometry. Quite a lot of the polypeptides were present in multiforms which indicated the presence of isoforms or the occurrence of post‐translational modifications. Among these proteins, we uncovered an abundant family that was identified as aldehyde dehydrogenases, representing approximately 7.5% of the soluble proteins. The comparative analysis of soluble mitochondrial proteomes led to the identification of a number of proteins which were specifically present in root or in seed mitochondria, thus revealing the impact of tissue differentiation at the mitochondrial level.