Os12g0555500
PBZ1, a PR10 family protein, has been shown to accumulate in tissues undergoing cell death/programmed cell death (PCD) in rice, it was first shown to be weakly induced only 3 days after treatment with a herbicide, probenazol.
Contents
Annotated Information
Function
PBZ1 gene has an important function during the disease resistance response in rice[1]. Numerous reports and researchers have hypothesized it as a molecular marker in rice self-defense, but the precise function of PBZ1 remains unknown[2][3][4]. In recent years, Sun et al. have demonstrated that the expression levels and localizations of PBZ1 dramatically coincided with tissues undergoing programmed cell death(PCD), namely, during leaf senescence, root aerenchyma formation, coleoptiles senescence, root cap, and seed aleurone layer[2].
- Naoki et al. have showed that the time course of the accumulation of the PBZl mRNA after treatment with probenazole corresponds to that of the development of anti-rice blast activity, this gene is somewhat related to disease resistance, and it is not a simple nonspecific response to chemical stimulation[1].
- Based on mRNA and protein analysis, Hideo et al, indicates that a promoter of PBZ1 is activated by salicylic acid(SA). What’s more, PBZ1 can also induced by jasmonic acid (JA), ethephon, abscisic acid (ABA), and NaCl[5].
Expression
Figure 1. Morphology of cell death. Dark brown color serves as an indica- tion of cell death(from reference[4]).
- Sang et al. found recombinant PBZ1 protein causes cell death in rice suspension-cultured cells(SCCs) and tobacco leaves. The result in Figure1, shows that suspended cells treated with PBZ1 protein turned into the dark brown color (i.e. cell death), whereas cells treated with others remained light yellow, suggesting that PBZ1 protein induces cell death in rice SCCs . The pre-immune serum did not cause any cell death. In planta, leaves of tobacco, cell death morphology was clearly visible within 72 h post application(Figure2). This phenomena can also find in Arabidopsis. What’s more they even found that rice cultured cells-treated with the PBZ1 protein reveal DNA fragmentation – a sign of PCD[4].
Mutation
Figure 2. (A) Does- dependent effect of PBZ1 protein on cell death. 1, 10 mM HEPES buffer (pH 7.0); 2, acetylated BSA (100 μg/ml); 3 through 6 are recombinant PBZ1 protein at the concentration of 10, 25, 50 and 100 μg/ml, respectively. (B) Cell death blocking experiment. 1, acetylated BSA (100 μg/mL); 2, PBZ1 antibody (10 μl); 3, PBZ1 protein (100 μg/ml); and 4, PBZ1 protein (100 μg/ml) plus PBZ1 antibody (10 μl). Numbers 1 and 2 serve as appropriate controls(from reference[4]).
- Mutation of a W-box like element in PBZ1 promoter abolished its SA inducibility. Because SA inducibility of the 687:LUC construct is the highest among deletion constructs, and only one WLE1 with the TGAC core is present in region III. If WLE1 in region III was mutagenized from TGAC to TGAA. The WRKY protein(it binds to the W boxes in rice, can regulate the defense signaling in rice) couldn’t bind to a TGAA sequence, therefore, this mutation prevents the association of WRKY to the WLE1 of the PBZ1 promoter, so this little mutation can abolish PBZ1’s SA inducibility[5].
Evolution
- Originally, OsPR10a was known to be induced by probenazole and thus, was called a probenazole-inducible gene, PBZ1. Later, PBZ1 was renamed as OsPR10a because it shares a similar sequence with (has sequence similarity to) PR-10 proteins[1][5].
Gene Structure
- The PBZ1 cDNA is 833 bp long and contain a major open reading frame of 474 bp that encode a putative protein of 158 amino acids with a predicted mol wt of 16,687 and a pi of 4.73. A putative polyadenylation signal (AATAAA) was found in the 3' non-coding region[1].
Labs working on this gene
- Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Korea
- Department of Plant Bioscience, Pusan National University, Busan 609-735, Korea
- United Graduate School, Tokyo Uni_ersity of Agriculture and Technology, Tokyo, Japan
- Food Function Laboratory, Ibaraki Uni_ersity, Ami, Ibaraki, Japan
- National Institute of Agricultural Biotechnology,Rural Development Administration,Suwon 440-707, South Korea
- Pharmaceutical Research Center, Meiji Seika Kaisha, Ltd., Morooka-cho, Kohoku-ku, Yokohama, 222 Japan
References
- ↑ 1.0 1.1 1.2 1.3 Midoh N, Iwata M. Cloning and characterization of a probenazole-inducible gene for an intracellular pathogenesis-related protein in rice[J]. Plant and cell physiology, 1996, 37(1): 9-18.
- ↑ 2.0 2.1 Kim S T, Kim S G, Kang Y H, et al. Proteomics analysis of rice lesion mimic mutant (spl 1) reveals tightly localized probenazole-induced protein (PBZ1) in cells undergoing programmed cell death[J]. Journal of proteome research, 2008, 7(4): 1750-1760.
- ↑ Rakwal R, Agrawal G K, Yonekura M. Light-dependent induction of OsPR10 in rice (Oryza sativa L.) seedlings by the global stress signaling molecule jasmonic acid and protein phosphatase 2A inhibitors[J]. Plant Science, 2001, 161(3): 469-479.
- ↑ 4.0 4.1 4.2 4.3 Kim S G, Kim S T, Wang Y, et al. The RNase activity of rice probenazole-induced protein1 (PBZ1) plays a key role in cell death in plants[J]. Molecules and cells, 2011, 31(1): 25-31.
- ↑ 5.0 5.1 5.2 Hwang S H, Lee I A, Yie S W, et al. Identification of an OsPR10a promoter region responsive to salicylic acid[J]. Planta, 2008, 227(5): 1141-1150.
