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Protein microarrays are a very attractive tool for functional proteomics due to the possibility of realizing a comprehensive analysis of the protein-protein interactions on a small scale. Such a microarray can provide a link between a specific biological function and the corresponding protein-protein interactions. The peptide microarrays of rice stripe virus coat protein have been successfully produced by our group, and the interactions of the coat protein with various viral proteins and host proteins were found on the array. Here, we designed and produced a series of peptide sequences containing single or multiple proline residues by using various amino acids. We further investigated the effects of these proline residues on the interactions of the coat protein with two host proteins, the Arabidopsis thaliana PP2C Ser/Thr protein phosphatase 2C and the Arabidopsis thaliana FLP/SYM protein histidine phosphatase 4, both of which are involved in plant stress responses. Our results indicated that the proline residue was beneficial for the interactions between coat protein and these two Arabidopsis proteins. To explore the characteristics of the isomerase domain of these two host proteins, we further characterized the GFP-PP2C and GFP-SYM fusion proteins, respectively. The results suggested that these two proteins can be divided into two categories: the proline-
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