1Department of Agricultural and Environmental Biology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
2Nano Medical Engineering Laboratory, RIKEN Cluster of Pioneering Research, Wako-shi, Saitama, Japan
3Faculty of Bioscience, Hosei University, Koganei-shi, Tokyo, Japan
*Corresponding author e-mail: Kensaku Maejima (amaejima@mail.ecc.u-tokyo.ac.jp)
Online published on 25 July, 2019.
Phyllody is one of the most characteristic symptoms associated with phytoplasmas, in which flower organs are transformed into leaf-like structures. A phytoplasma conserved effector, called phyllogen (phyllody-inducing gene family), works as a phyllody inducer by degrading floral MADS-domain transcription factors (MTFs). In this study the crystal structure of PHYL1OY, a phyllogen of ‘Candidatus Phytoplasma asteris’ onion yellows strain, was elucidated at a resolution of 2.4 Å. PHYL1OY, is formed by two α-helices connected by a random loop in a coiled-coil manner. Other phyllogens were also predicted to contain two consensus α-helices. Amino acid insertion mutations into either α-helix of PHYL1OY disrupted its phyllody-inducing activity and ability to degrade MTF, although the same insertion in the loop region did not affect either. These results indicated that both conserved α-helices are important for the function of phyllogen.
Phyllody, phyllogen, crystal structure, MADS-domain transcription factors, α-helix