The structure of Arabidopsis phytochrome A reveals topological and functional diversification among the plant photoreceptor isoforms.


Journal

Nature plants
ISSN: 2055-0278
Titre abrégé: Nat Plants
Pays: England
ID NLM: 101651677

Informations de publication

Date de publication:
07 2023
Historique:
received: 14 12 2022
accepted: 10 05 2023
medline: 21 7 2023
pubmed: 9 6 2023
entrez: 8 6 2023
Statut: ppublish

Résumé

Plants employ a divergent cohort of phytochrome (Phy) photoreceptors to govern many aspects of morphogenesis through reversible photointerconversion between inactive Pr and active Pfr conformers. The two most influential are PhyA whose retention of Pfr enables sensation of dim light, while the relative instability of Pfr for PhyB makes it better suited for detecting full sun and temperature. To better understand these contrasts, we solved, by cryo-electron microscopy, the three-dimensional structure of full-length PhyA as Pr. Like PhyB, PhyA dimerizes through head-to-head assembly of its C-terminal histidine kinase-related domains (HKRDs), while the remainder assembles as a head-to-tail light-responsive platform. Whereas the platform and HKRDs associate asymmetrically in PhyB dimers, these lopsided connections are absent in PhyA. Analysis of truncation and site-directed mutants revealed that this decoupling and altered platform assembly have functional consequences for Pfr stability of PhyA and highlights how plant Phy structural diversification has extended light and temperature perception.

Identifiants

pubmed: 37291396
doi: 10.1038/s41477-023-01435-8
pii: 10.1038/s41477-023-01435-8
pmc: PMC10546791
mid: NIHMS1928402
doi:

Substances chimiques

Arabidopsis Proteins 0
Photoreceptors, Plant 0
Phytochrome 11121-56-5
Phytochrome A 0
Phytochrome B 136250-22-1
Protein Isoforms 0
PHYA protein, Arabidopsis 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1116-1129

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM127892
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131754
Pays : United States

Informations de copyright

© 2023. The Author(s), under exclusive licence to Springer Nature Limited.

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Auteurs

E Sethe Burgie (ES)

Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.

Hua Li (H)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Zira T K Gannam (ZTK)

Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.

Katrice E McLoughlin (KE)

Department of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Burning Rock Dx, Irvine, CA, USA.

Richard D Vierstra (RD)

Department of Biology, Washington University in St. Louis, St. Louis, MO, USA. rdvierstra@wustl.edu.

Huilin Li (H)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA. Huilin.Li@vai.org.

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Classifications MeSH