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Plant Molecular Biology

, Volume 99, Issue 1–2, pp 135–148 | Cite as

Post-translational and transcriptional regulation of phenylpropanoid biosynthesis pathway by Kelch repeat F-box protein SAGL1

  • Si-in Yu
  • Hyojin Kim
  • Dae-Jin Yun
  • Mi Chung Suh
  • Byeong-ha LeeEmail author
Article
  • 258 Downloads

Abstract

Key message

A Kelch repeat F-box containing protein, SMALL AND GLOSSY LEAVES1 (SAGL1) regulates phenylpropanoid biosynthesis as a post-translational regulator for PAL1 (phenylalanine ammonia-lyase) and an indirect transcriptional regulator for ANTHOCYANIDIN SYNTHASE.

Abstract

Phenylpropanoid biosynthesis in plants produces diverse aromatic metabolites with important biological functions. Phenylalanine ammonia-lyase (PAL) catalyzes the first step in phenylpropanoid biosynthesis by converting l-phenylalanine to trans-cinnamic acid. Here, we report that SMALL AND GLOSSY LEAVES1 (SAGL1), a Kelch repeat F-box protein, interacts with PAL1 protein for proteasome-mediated degradation to regulate phenylpropanoid biosynthesis in Arabidopsis. Mutations in SAGL1 caused high accumulation of anthocyanins and lignin derived from the phenylpropanoid biosynthesis pathway. We found that PAL enzyme activity increased in SAGL1-defective mutants, sagl1, but decreased in SAGL1-overexpressing Arabidopsis (SAGL1OE) without changes in the transcript levels of PAL genes, suggesting protein-level regulation by SAGL1. Indeed, the levels of PAL1-GFP fusion protein were reduced when both SAGL1 and PAL1-GFP were transiently co-expressed in leaves of Nicotiana benthamiana. In addition, bimolecular fluorescence complementation analysis suggested an interaction between SAGL1 and PAL1. We also found that the transcript levels of ANTHOCYANIDIN SYNTHASE (ANS) increased in the sagl1 mutants but decreased in SAGL1OE. Our results suggest that SAGL1 regulates phenylpropanoid biosynthesis post-translationally at PAL1 and transcriptionally at ANS.

Keywords

Phenylpropanoid biosynthesis Kelch repeat F-box protein Phenylalanine ammonia-lyase Anthocyanin Lignin 

Notes

Acknowledgements

This research was supported by Basic Science Research Program (NRF-2016R1D1A1B03933195) and Global Research Laboratory Program (2017K1A1A2013146) through the National Research Foundation of Korea (NRF) funded by the Ministry of Education and the Ministry of Science and ICT (MSIT), South Korea.

Author Contributions

BhL and MCS conceived and designed the experiments. SiY and HK conducted experiments. SiY, HK, DJY, MCS and BhL discussed and interpreted the results. SiY and BhL wrote the paper with the help of HK, DJY and MCS.

Compliance with ethical standards

Conflict interest

The authors declare no conflict of interest.

Supplementary material

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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  1. 1.Department of Life ScienceSogang UniversitySeoulRepublic of Korea
  2. 2.Department of Biomedical Science and EngineeringKonkuk UniversitySeoulRepublic of Korea

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