Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors

Yi Ting Liao, Shih Shun Lin, Shin Jen Lin, Wan Ting Sun, Bing Nan Shen, Han Pin Cheng, Chan Pin Lin, Tzu Ping Ko, Yi Fan Chen, Hao Ching Wang

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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 (PHYL1) 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 PHYL1 has prevented a detailed understanding of the binding mechanism between PHYL1 and the MADS transcription factors. Here, we present the crystal structure of PHYL1 from peanut witches’-broom phytoplasma (PHYL1Pn 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 PHYL1Pn WB with the K domain of the MADS transcription factor SEPALLATA3 (SEP3_K) and identify the residues of PHYL1Pn WB that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1Pn WB proteins to SEP3_K. Lastly, based on confocal images, we found that α-helix 2 of PHYL1Pn WB plays an important role in PHYL1-mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1Pn WB and SEP3_K.

Original languageEnglish
JournalPlant Journal
DOIs
Publication statusAccepted/In press - Jan 1 2019

Fingerprint

Peanut witches'-broom phytoplasma
Phytoplasma
Transcription Factors
transcription factors
surface plasmon resonance
dwarfing
keratin
papayas
crystal structure
Carica
Dwarfism
plant pathogens
proteomics
signs and symptoms (plants)
Plant Development
peanuts
Surface Plasmon Resonance
plant development
proteins
Keratins

Keywords

  • MADS transcription factor
  • Phytoplasma
  • Phytoplasmal effector causing phyllody 1

ASJC Scopus subject areas

  • Genetics
  • Plant Science
  • Cell Biology

Cite this

Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors. / Liao, Yi Ting; Lin, Shih Shun; Lin, Shin Jen; Sun, Wan Ting; Shen, Bing Nan; Cheng, Han Pin; Lin, Chan Pin; Ko, Tzu Ping; Chen, Yi Fan; Wang, Hao Ching.

In: Plant Journal, 01.01.2019.

Research output: Contribution to journalArticle

Liao, Yi Ting ; Lin, Shih Shun ; Lin, Shin Jen ; Sun, Wan Ting ; Shen, Bing Nan ; Cheng, Han Pin ; Lin, Chan Pin ; Ko, Tzu Ping ; Chen, Yi Fan ; Wang, Hao Ching. / Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors. In: Plant Journal. 2019.
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abstract = "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 (PHYL1) 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 PHYL1 has prevented a detailed understanding of the binding mechanism between PHYL1 and the MADS transcription factors. Here, we present the crystal structure of PHYL1 from peanut witches’-broom phytoplasma (PHYL1Pn 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 PHYL1Pn WB with the K domain of the MADS transcription factor SEPALLATA3 (SEP3_K) and identify the residues of PHYL1Pn WB that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1Pn WB proteins to SEP3_K. Lastly, based on confocal images, we found that α-helix 2 of PHYL1Pn WB plays an important role in PHYL1-mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1Pn WB and SEP3_K.",
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AB - 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 (PHYL1) 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 PHYL1 has prevented a detailed understanding of the binding mechanism between PHYL1 and the MADS transcription factors. Here, we present the crystal structure of PHYL1 from peanut witches’-broom phytoplasma (PHYL1Pn 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 PHYL1Pn WB with the K domain of the MADS transcription factor SEPALLATA3 (SEP3_K) and identify the residues of PHYL1Pn WB that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1Pn WB proteins to SEP3_K. Lastly, based on confocal images, we found that α-helix 2 of PHYL1Pn WB plays an important role in PHYL1-mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1Pn WB and SEP3_K.

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