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A proteomic analysis of organelles from Arabidopsis thaliana
Author(s) -
Prime Tracy A.,
Sherrier D. Janine,
Mahon Piers,
Packman Len C.,
Dupree Paul
Publication year - 2000
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(20001001)21:16<3488::aid-elps3488>3.0.co;2-3
Subject(s) - organelle , callus , proteome , endoplasmic reticulum , golgi apparatus , proteomics , arabidopsis thaliana , arabidopsis , microbiology and biotechnology , membrane protein , biochemistry , chemistry , biology , two dimensional gel electrophoresis , gel electrophoresis , membrane , botany , mutant , gene
We introduce the use of Arabidopsis thaliana callus culture as a system for proteomic analysis of plant organelles using liquid‐grown callus. This callus is relatively homogeneous, reproducible and cytoplasmically rich, and provides organelles in sufficient quantities for proteomic studies. A database was generated of mitochondrial, endoplasmic reticulum (ER), Golgi/prevacuolar compartment and plasma membrane (PM) markers using two‐dimensional sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (2‐D SDS‐PAGE) and peptide sequencing or mass spectrometric methods. The major callus membrane‐associated proteins were characterised as being integral or peripheral by Triton X‐114 phase partitioning. The database was used to define specific proteins at the Arabidopsis callus plasma membrane. This database of organelle proteins provides the basis for future characterisation of the expression and localisation of novel plant proteins.