Structural insights into the photoactivation of Arabidopsis CRY2.

Nature Plants
Ling MaPing Yin

Abstract

The blue-light receptor cryptochrome (CRY) in plants undergoes oligomerization to transduce blue-light signals after irradiation, but the corresponding molecular mechanism remains poorly understood. Here, we report the cryogenic electron microscopy structure of a blue-light-activated CRY2 tetramer at a resolution of 3.1 Å, which shows how the CRY2 tetramer assembles. Our study provides insights into blue-light-mediated activation of CRY2 and a theoretical basis for developing regulators of CRYs for optogenetic manipulation.

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Citations

Jun 9, 2021·The Journal of Physical Chemistry Letters·Lukas Goett-ZinkTilman Kottke
Mar 17, 2021·Annual Review of Biomedical Engineering·Payam E FarahaniJared E Toettcher

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Datasets Mentioned

BETA
30023

Methods Mentioned

BETA
gel filtration
size-exclusion chromatography
electron microscopy
transgenic
pull-down
light scattering

Software Mentioned

MotionCor2
Gctf
POVME
ImageJ
MolProbity
MotionCorr2
Phenix
COOT
RELION3

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