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Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors
Author(s) -
Liao YiTing,
Lin ShihShun,
Lin ShinJen,
Sun WanTing,
Shen BingNan,
Cheng HanPin,
Lin ChanPin,
Ko TzuPing,
Chen YiFan,
Wang HaoChing
Publication year - 2019
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.14463
Subject(s) - phyllody , transcription factor , virescence , effector , phytoplasma , biology , microbiology and biotechnology , genetics , computational biology , botany , polymerase chain reaction , gene , restriction fragment length polymorphism
Summary Phytoplasmas are bacterial plant pathogens which can induce severe symptoms including dwarfism, phyllody and virescence in an infected plant. Because phytoplasmas infect many important crops such as peanut and papaya they have caused serious agricultural losses. The phytoplasmal effector causing phyllody 1 ( PHYL 1) is an important phytoplasmal pathogenic factor which affects the biological function of MADS transcription factors by interacting with their K (keratin‐like) domain, thus resulting in abnormal plant developments such as phyllody. Until now, lack of information on the structure of PHYL 1 has prevented a detailed understanding of the binding mechanism between PHYL 1 and the MADS transcription factors. Here, we present the crystal structure of PHYL 1 from peanut witches’‐broom phytoplasma ( PHYL 1 Pn WB ). This protein was found to fold into a unique α‐helical hairpin with exposed hydrophobic residues on its surface that may play an important role in its biological function. Using proteomics approaches, we propose a binding mode of PHYL 1 Pn WB with the K domain of the MADS transcription factor SEPALLATA 3 ( SEP 3_K) and identify the residues of PHYL 1 Pn WB that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL 1 Pn WB proteins to SEP 3_K. Lastly, based on confocal images, we found that α‐helix 2 of PHYL 1 Pn WB plays an important role in PHYL 1‐mediated degradation of SEP 3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL 1 Pn WB and SEP 3_K.