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Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors.
- Source :
-
The Plant journal : for cell and molecular biology [Plant J] 2019 Nov; Vol. 100 (4), pp. 706-719. Date of Electronic Publication: 2019 Sep 09. - Publication Year :
- 2019
-
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 (PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> ). 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 PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> with the K domain of the MADS transcription factor SEPALLATA3 (SEP3&#95;K) and identify the residues of PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> proteins to SEP3&#95;K. Lastly, based on confocal images, we found that α-helix 2 of PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> plays an important role in PHYL1-mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1 <subscript>Pn</subscript> <subscript>WB</subscript> and SEP3&#95;K.<br /> (© 2019 The Authors The Plant Journal © 2019 John Wiley & Sons Ltd.)
- Subjects :
- Bacterial Proteins genetics
Bacterial Proteins metabolism
Cross-Linking Reagents chemistry
Crystallography, X-Ray
Host-Pathogen Interactions physiology
Hydrophobic and Hydrophilic Interactions
MADS Domain Proteins chemistry
MADS Domain Proteins genetics
Multiprotein Complexes chemistry
Mutation
Phytoplasma pathogenicity
Plant Diseases microbiology
Plant Proteins chemistry
Plant Proteins genetics
Protein Interaction Domains and Motifs
Bacterial Proteins chemistry
MADS Domain Proteins metabolism
Phytoplasma chemistry
Plant Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1365-313X
- Volume :
- 100
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- The Plant journal : for cell and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 31323156
- Full Text :
- https://doi.org/10.1111/tpj.14463