Functional characterization of PRPD and PRMS in Arabidopsis

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Functional characterization of PRPD and PRMS in Arabidopsis thaliana
Seong_Yeon Park, Mei Hua Cui, Jun Young Choi and Jeong Sheop Shin
Department of Life Sciences, Korea University, Seoul 136-701, Republic of Korea
Appropriate stamen development is a significant process in plants to continue their life
cycles. Defects in stamen development will cause male sterility. One of factors that affect
male sterility is the defective and abnormal pollen development. In this study, we
characterized physiological functions of two proteins. The one is the Protein Related to the
Pollen Development (PRPD) that has a sugar isomerase domain as well as a single
cystathionine ß-synthase (CBS) domain. We expected that PRPD has similar function with
GutQ that is a arabinose-5-phosphate isomerase in Escherichia coli and that PRPD may be
involved in pollen development according to the Genevestigator expression data. . The other
is Protein Related to the Male Sterility (PRMS), which is a transcription factor containing
cysteine-rich domains. We observed that PRPD and PRMS expressed strongly in flowers. We
identified that these promoters strongly drive GUS expression in anthers rather than other
tissues using ProPRPD:GUS and ProPRMS:GUS transgenic lines. Microscopic observation
of 35S:PRPD-smGFP in transgenic Arabidopsis revealed that it localizes to nucleus and
plasma membrane, while 35S:PRMS-smGFP localizes solely to nucleus, as a transcription
factor. We confirmed that PRPD expression was decreased in drought, cytokinin and
hydrogen peroxide treatments, but showed similar expression patterns under ABA, NaCl and
salicylic acid treatments compared to the wild type. However, PRMS was increased in NaCl,
ABA and drought stresses but decreased under salicylic acid treatment. Moreover, 35S:PRMS
transgenic plants showed male sterile phenotype. We further investigated and suggested the
possible functional roles of these two proteins in various abiotic stresses and plant stamen
development.
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