First published online February 6, 2003; 10.1104/pp.102.015362
Plant Physiol, March 2003, Vol. 131, pp. 1080-1090
Proteome Analysis. Novel Proteins Identified at the Peribacteroid
Membrane from Lotus japonicus Root
Nodules1
Stefanie
Wienkoop2 and
Gerhard
Saalbach*
Department of Plant Research, Risø National Laboratory, Roskilde,
Denmark
The peribacteroid membrane (PBM) forms the structural and
functional interface between the legume plant and the rhizobia. The
model legume Lotus japonicus was chosen to study the
proteins present at the PBM by proteome analysis. PBM was purified from root nodules by an aqueous polymer two-phase system. Extracted proteins
were subjected to a global trypsin digest. The peptides were separated
by nanoscale liquid chromatography and analyzed by tandem mass
spectrometry. Searching the nonredundant protein database and the green
plant expressed sequence tag database using the tandem mass
spectrometry data identified approximately 94 proteins, a number far
exceeding the number of proteins reported for the PBM hitherto. In
particular, a number of membrane proteins like transporters for sugars
and sulfate; endomembrane-associated proteins such as GTP-binding
proteins and vesicle receptors; and proteins involved in signaling, for
example, receptor kinases, calmodulin, 14-3-3 proteins, and pathogen
response-related proteins, including a so-called HIR protein, were
detected. Several ATPases and aquaporins were present, indicating a
more complex situation than previously thought. In addition, the
unexpected presence of a number of proteins known to be located in
other compartments was observed. Two characteristic protein complexes
obtained from native gel electrophoresis of total PBM proteins were
also analyzed. Together, the results identified specific proteins at
the PBM involved in important physiological processes and localized
proteins known from nodule-specific expressed sequence tag databases to the PBM.
1
This work was supported by a 2-year trainee
program of the European Union research training network Lotus (to
S.W.).
2
Present address: Max Planck Institute of
Molecular Plant Physiology, Am Mühlenberg 1, D-14476 Golm, Germany.
*
Corresponding author; e-mail G.Saalbach{at}risoe.dk; fax
45-4677-4282.
© 2003 American Society of Plant Biologists
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