Structural basis of JAZ repression of MYC transcription factors in jasmonate signalling.

dc.contributor.author

Zhang, Feng

dc.contributor.author

Yao, Jian

dc.contributor.author

Ke, Jiyuan

dc.contributor.author

Zhang, Li

dc.contributor.author

Lam, Vinh Q

dc.contributor.author

Xin, Xiu-Fang

dc.contributor.author

Zhou, X Edward

dc.contributor.author

Chen, Jian

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Brunzelle, Joseph

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Griffin, Patrick R

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Zhou, Mingguo

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Xu, H Eric

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Melcher, Karsten

dc.contributor.author

He, Sheng Yang

dc.date.accessioned

2020-11-25T23:00:31Z

dc.date.available

2020-11-25T23:00:31Z

dc.date.issued

2015-09

dc.date.updated

2020-11-25T23:00:28Z

dc.description.abstract

The plant hormone jasmonate plays crucial roles in regulating plant responses to herbivorous insects and microbial pathogens and is an important regulator of plant growth and development. Key mediators of jasmonate signalling include MYC transcription factors, which are repressed by jasmonate ZIM-domain (JAZ) transcriptional repressors in the resting state. In the presence of active jasmonate, JAZ proteins function as jasmonate co-receptors by forming a hormone-dependent complex with COI1, the F-box subunit of an SCF-type ubiquitin E3 ligase. The hormone-dependent formation of the COI1-JAZ co-receptor complex leads to ubiquitination and proteasome-dependent degradation of JAZ repressors and release of MYC proteins from transcriptional repression. The mechanism by which JAZ proteins repress MYC transcription factors and how JAZ proteins switch between the repressor function in the absence of hormone and the co-receptor function in the presence of hormone remain enigmatic. Here we show that Arabidopsis MYC3 undergoes pronounced conformational changes when bound to the conserved Jas motif of the JAZ9 repressor. The Jas motif, previously shown to bind to hormone as a partly unwound helix, forms a complete α-helix that displaces the amino (N)-terminal helix of MYC3 and becomes an integral part of the MYC N-terminal fold. In this position, the Jas helix competitively inhibits MYC3 interaction with the MED25 subunit of the transcriptional Mediator complex. Our structural and functional studies elucidate a dynamic molecular switch mechanism that governs the repression and activation of a major plant hormone pathway.

dc.identifier

nature14661

dc.identifier.issn

0028-0836

dc.identifier.issn

1476-4687

dc.identifier.uri

https://hdl.handle.net/10161/21722

dc.language

eng

dc.publisher

Springer Science and Business Media LLC

dc.relation.ispartof

Nature

dc.relation.isversionof

10.1038/nature14661

dc.subject

Arabidopsis

dc.subject

Cyclopentanes

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Proteasome Endopeptidase Complex

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Plant Growth Regulators

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Apoproteins

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Trans-Activators

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Nuclear Proteins

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Arabidopsis Proteins

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Repressor Proteins

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Crystallography, X-Ray

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Signal Transduction

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Binding, Competitive

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Amino Acid Motifs

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Protein Conformation

dc.subject

Protein Binding

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Models, Molecular

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Ubiquitination

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Oxylipins

dc.title

Structural basis of JAZ repression of MYC transcription factors in jasmonate signalling.

dc.type

Journal article

duke.contributor.orcid

He, Sheng Yang|0000-0003-1308-498X

pubs.begin-page

269

pubs.end-page

273

pubs.issue

7568

pubs.organisational-group

Trinity College of Arts & Sciences

pubs.organisational-group

Biology

pubs.organisational-group

Duke

pubs.publication-status

Published

pubs.volume

525

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