Crystal structure of phyllogen, a phyllody-inducing effector protein of phytoplasma

Iwabuchi, Nozomu; Maejima, Kensaku; Kitazawa, Yugo; Miyatake, Hideyuki; Nishikawa, Manabu; Tokuda, Ryosuke; Koinuma, Hiroaki; Miyazaki, Akio; Nijo, Takamichi; Oshima, Kenro; Yamaji, Yutaka; Namba, Susumu

doi:10.1016/j.bbrc.2019.04.060

Cited by 30 publications

(84 citation statements)

References 28 publications

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“…The crystal structure of the PHYL1 homolog from onion yellows (PHYL1 OY ) has recently been reported (Iwabuchi et al, 2019). Although the sequence similarity between PHYL1 PnWB and PHYL1 OY is only 60%, both proteins are folded into similar conformations ( Figure S11).…”

Section: Discussionmentioning

confidence: 99%

“…The only difference is found in PHYL1 PnWB Y32, this residue may be important for targeting specific MADS transcription factors, as hypothesized above. In the study of PHYL1 OY , Iwabuchi et al (2019) selected four conserved amino acids (PHYL1 OY K28, P53, L68 and Q75) and used amino acid insertion to confirm that three of them (PHYL1 OY K28, L68 and Q75) were important for interacting MADS transcription factor as well as for RAD23 binding. We note with interest that these three amino acids are also conserved in PHYL1 PnWB (Figure S11c).…”

Section: Discussionmentioning

confidence: 99%

“…We note with interest that these three amino acids are also conserved in PHYL1 PnWB (Figure S11c). However, the technique of amino acid insertion that was used in the PHYL1 OY study was also described as producing an axial rotational shift of 200°in the a-helices (Iwabuchi et al, 2019). Since this rotation could also result in other important hydrophobic residues moving from the outside to the inside of the hairpin, the actual importance of these three residues should be carefully confirmed.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, the effectors that induce phyllody have been collectively labeled as phyllogens (Maejima et al, 2014). These phyllogens include the secreted aster yellows witches'-broom (AYWB) phytoplasma protein 54 (SAP54) and its close homolog, phytoplasmal effector causing phyllody symptoms 1, from onion yellows phytoplasma (PHYL1 OY ) and peanut witches'-broom phytoplasma (PHYL1 PnWB ) (MacLean et al, 2011;Maejima et al, 2014Maejima et al, , 2015Liu et al, 2015;Yang et al, 2015;Iwabuchi et al, 2019). The PHYL1 homologs PHYL1 OY and SAP54 have recently been shown to interact with Arabidopsis SEPALLATA1-4 (SEP1-4) and APETALA1 (AP1), both of which are MADS domain transcription factors that are assumed to be essential components of the floral quartets (MacLean et al, 2014;Maejima et al, 2014Maejima et al, , 2015.…”

Section: Introductionmentioning

confidence: 99%

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

Liao

Lin

et al. 2019

The Plant Journal

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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 (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 (PHYL1PnWB). 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 PHYL1PnWB with the K domain of the MADS transcription factor SEPALLATA3 (SEP3_K) and identify the residues of PHYL1PnWB that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1PnWB proteins to SEP3_K. Lastly, based on confocal images, we found that α‐helix 2 of PHYL1PnWB plays an important role in PHYL1‐mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1PnWB and SEP3_K.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Liao

Lin

et al. 2019

The Plant Journal

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“…While this manuscript was in preparation, Iwabuchi et al (2019) PHYL1OY shares about 87 % sequence identity with SAP54 ( Figure 1a) and generates similar symptoms in planta, suggesting that both proteins work in very similar ways (Maejima et al, 2014). In contrast, PHYL1PnWB shares only about 53% sequence identity with SAP54 and is hence probably more distantly related than PHYL1OY (Figure 1a; Liao et al, 2019).…”

Section: Discussionmentioning

confidence: 97%

Structural requirements of the phytoplasma effector protein SAP54 for causing homeotic transformation of floral organs

Aurin¹,

Haupt

Goerlach

et al. 2019

Preprint

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SIGNIFICANCE STATEMENTPhytoplasmas are bacterial plant pathogens that cause devastating diseases in crops and ornamental plants by the secretion of effector proteins such as SAP54, which leads to the degradation of some floral homeotic proteins. Our study clarifies the structural requirements of SAP54 function and illuminates the molecular mode of interaction and thus may ultimately help to develop treatments against some devastating plant diseases. SummaryPhytoplasmas are intracellular bacterial plant pathogens that cause devastating diseases in crops and ornamental plants by the secretion of effector proteins. One of these effector proteins, termed SECRETED ASTER YELLOWS-WITCHES' BROOM PROTEIN 54 (SAP54), leads to the degradation of a specific subset of floral homeotic proteins of the MIKC-type MADSdomain family via the ubiquitin-proteasome pathway. In consequence, the developing flowers show the homeotic transformation of floral organs into vegetative leaf-like structures. The molecular mechanism of SAP54 action involves physical binding to the keratin-like K-domain of MIKC-type proteins, and to some RAD23 proteins, which translocate ubiquitylated substrates to the proteasome. The structural requirements and specificity of SAP54 function are poorly understood, however. Here we report, based on biophysical and molecular biological analyses, that SAP54 folds into α-helical structures. We also show that the insertion of helixbreaking mutations disrupts correct folding of SAP54, which interferes with the ability of SAP54 to bind to its target proteins and to cause disease phenotypes in vivo. Surprisingly, dynamic light scattering data together with electrophoretic mobility shift assays suggest that SAP54 preferentially binds to multimeric complexes of MIKC-type proteins rather than to dimers or monomers of these proteins. Together with literature data this finding suggests that MIKC-type proteins and SAP54 constitute multimeric α-helical coiled-coils, possibly also involving other partners such as RAD23 proteins. Our investigations clarify the structurefunction relationship of an important phytoplasma effector protein and thus may ultimately help to develop treatments against some devastating plant diseases.

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Molecular biological study on the survival strategy of phytoplasma

Oshima

2021

J Gen Plant Pathol

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Crystal structure of phyllogen, a phyllody-inducing effector protein of phytoplasma

Cited by 30 publications

References 28 publications

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

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

Structural requirements of the phytoplasma effector protein SAP54 for causing homeotic transformation of floral organs

Molecular biological study on the survival strategy of phytoplasma

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