Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein

Changin Kim, So Ri Yun, Sang Jin Lee, Seong Ok Kim, Hyosub Lee, Jungkweon Choi, Jong Goo Kim, Tae Wu Kim, Seyoung You, Irina Kosheleva, Taeyoon Noh, Jonghoon Baek and Hyotcherl Ihee ()
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Changin Kim: Korea Advanced Institute of Science and Technology (KAIST)
So Ri Yun: Korea Advanced Institute of Science and Technology (KAIST)
Sang Jin Lee: Korea Advanced Institute of Science and Technology (KAIST)
Seong Ok Kim: Korea Advanced Institute of Science and Technology (KAIST)
Hyosub Lee: Korea Advanced Institute of Science and Technology (KAIST)
Jungkweon Choi: Korea Advanced Institute of Science and Technology (KAIST)
Jong Goo Kim: Korea Advanced Institute of Science and Technology (KAIST)
Tae Wu Kim: Korea Advanced Institute of Science and Technology (KAIST)
Seyoung You: Korea Advanced Institute of Science and Technology (KAIST)
Irina Kosheleva: The University of Chicago
Taeyoon Noh: Korea Advanced Institute of Science and Technology (KAIST)
Jonghoon Baek: Korea Advanced Institute of Science and Technology (KAIST)
Hyotcherl Ihee: Korea Advanced Institute of Science and Technology (KAIST)

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract The Light-oxygen-voltage-sensing domain (LOV) superfamily, found in enzymes and signal transduction proteins, plays a crucial role in converting light signals into structural signals, mediating various biological mechanisms. While time-resolved spectroscopic studies have revealed the dynamics of the LOV-domain chromophore’s electronic structures, understanding the structural changes in the protein moiety, particularly regarding light-induced dimerization, remains challenging. Here, we utilize time-resolved X-ray liquidography to capture the light-induced dimerization of Avena sativa LOV2. Our analysis unveils that dimerization occurs within milliseconds after the unfolding of the A’α and Jα helices in the microsecond time range. Notably, our findings suggest that protein-protein interactions (PPIs) among the β-scaffolds, mediated by helix unfolding, play a key role in dimerization. In this work, we offer structural insights into the dimerization of LOV2 proteins following structural changes in the A’α and Jα helices, as well as mechanistic insights into the protein-protein association process driven by PPIs.

Date: 2024
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DOI: 10.1038/s41467-024-51461-z

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