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Structural mechanism of signal transduction in a phytochrome histidine kinase

Year of publication

2022

Authors

Wahlgren, Weixiao Yuan; Claesson, Elin; Tuure, Iida; Trillo-Muyo, Sergio; Bódizs, Szabolcs; Ihalainen, Janne A.; Takala, Heikki; Westenhoff, Sebastian

Abstract

Phytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its tertiary domain arrangement, but the connector helices between the photosensory and the histidine kinase modules open up like a zipper, causing asymmetry and disorder in the effector domains. The structures provide a framework for atom-scale understanding of signaling in phytochromes, visualize allosteric communication over several nanometers, and suggest that disorder in the dimeric arrangement of the effector domains is important for phosphatase activity in a two-component system. The results have implications for the development of optogenetic applications.
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Organizations and authors

University of Jyväskylä

Takala Heikki Orcid -palvelun logo

Tuure Iida Orcid -palvelun logo

Ihalainen Janne Orcid -palvelun logo

University of Helsinki

Takala Heikki

Publication type

Publication format

Article

Parent publication type

Journal

Article type

Original article

Audience

Scientific

Peer-reviewed

Peer-Reviewed

MINEDU's publication type classification code

A1 Journal article (refereed), original research

Publication channel information

Parent publication name

Nature Communications

Volume

13

Issue

1

Article number

7673

​Publication forum

63766

​Publication forum level

3

Open access

Open access in the publisher’s service

Yes

Open access of publication channel

Fully open publication channel

Self-archived

Yes

Other information

Fields of science

Plant biology, microbiology, virology; Biomedicine

Keywords

[object Object],[object Object],[object Object]

Publication country

United Kingdom

Internationality of the publisher

International

Language

English

International co-publication

Yes

Co-publication with a company

No

DOI

10.1038/s41467-022-34893-3

The publication is included in the Ministry of Education and Culture’s Publication data collection

Yes