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Phytochrome signalling is mediated through nucleoside diphosphate kinase 2

Abstract

Because plants are sessile, they have developed intricate strategies to adapt to changing environmental variables, including light. Their growth and development, from germination to flowering, is critically influenced by light, particularly at red (660 nm) and far-red (730 nm) wavelengths1,2. Higher plants perceive red and far-red light by means of specific light sensors called phytochromes(A–E)3. However, very little is known about how light signals are transduced to elicit responses in plants. Here we report that nucleoside diphosphate kinase 2 (NDPK2) is an upstream component in the phytochrome signalling pathway in the plant Arabidopsis thaliana. In animal and human cells, NDPK acts as a tumour suppressor4. We show that recombinant NDPK2 in Arabidopsis preferentially binds to the red-light-activated form of phytochrome in vitro and that this interaction increases the activity of recombinant NDPK2. Furthermore, a mutant lacking NDPK2 showed a partial defect in responses to both red and far-red light, including cotyledon opening and greening. These results indicate that NDPK2 is a positive signalling component of the phytochrome-mediated light-signal-transduction pathway in Arabidopsis.

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Figure 1: NDPK2 interacts preferentially with the Pfr form of phytochrome, whereas NDPK1 and NDPK3 do not interact.
Figure 2: Subcellular localization of NDPK2.
Figure 3: The Pfr-dependent activation of the recombinant Arabidopsis NDPK2.
Figure 4: Far-red high-irradiance response of a ndpk2 mutant.
Figure 5: Red-light high-irradiance response of a ndpk2 mutant.

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Acknowledgements

This work was supported by the Kumho Petrochemical Co., the Korea Science and Engineering Foundation, The Academic Research Fund of the Ministry of Education, Republic of Korea and USPHS-NIH. We thank the Arabidopsis Stock Centre for sending seeds.

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Correspondence to Giltsu Choi.

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Choi, G., Yi, H., Lee, J. et al. Phytochrome signalling is mediated through nucleoside diphosphate kinase 2. Nature 401, 610–613 (1999). https://doi.org/10.1038/44176

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