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Abstract
The proteome of a salinity-tolerant Arachis hypogaea L. callus cell line was compared with its sensitive counterpart. Several low molecular weight proteins were detected by two-dimensional electrophoresis as being unique or significantly elevated in the tolerant line. The identities of several of these proteins were established as PR 10 proteins using tandem Mass Spectrometry and are shown to be phosphorylated on the basis of staining with the phosphorylation-specific stain, Pro-Q Diamond. Our results suggest that these differentially phosphorylated PR 10 proteins may play an important role in mediating salinity stress responses.
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