Unusual photodynamic characteristics of the light-oxygen-voltage domain of phototropin linked to terrestrial adaptation of Klebsormidium nitens.

Autor: Sharma S; Laboratory of Optobiotechnology, School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.; Department of Cellular Biology, University of Georgia, Athens, Georgia, USA., Gautam AK; Structural Biology Lab, School of Life Sciences, Jawaharlal Nehru University, New Delhi, India., Singh R; Laboratory of Optobiotechnology, School of Biotechnology, Jawaharlal Nehru University, New Delhi, India., Gourinath S; Structural Biology Lab, School of Life Sciences, Jawaharlal Nehru University, New Delhi, India., Kateriya S; Laboratory of Optobiotechnology, School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.
Jazyk: angličtina
Zdroj: The FEBS journal [FEBS J] 2024 Dec; Vol. 291 (23), pp. 5156-5176. Date of Electronic Publication: 2024 Sep 29.
DOI: 10.1111/febs.17284
Abstrakt: Phototropin (Phot), a blue light-sensing LOV domain protein, mediates blue light responses and is evolutionarily conserved across the green lineage. Klebsormidium nitens, a green terrestrial alga, presents a valuable opportunity to study adaptive responses from aquatic to land habitat transitions. We determined the crystal structure of Klebsormidium nitens Phot LOV1 domain (KnLOV1) in the dark and engineered different mutations (R60K, Q122N, and D33N) to modulate the lifetime of the photorecovery cycle. We observed unusual, slow recovery kinetics in the wild-type KnLOV1 domain (τ = 41 ± 3 min) compared to different mutants (R60K: τ = 2.0 ± 0.1 min, Q122N: τ = 1.7 ± 0.1 min, D33N: τ = 9.6 ± 0.1 min). Crystal structures of wild-type KnLOV1 and mutants revealed subtle but critical changes near the protein chromophore that is responsible for modulating protein dark recovery time. Our findings shed light on the unique structural and biochemical characteristics of the newly studied KnLOV1 and its evolutionary importance for phototropin-mediated physiology.
(© 2024 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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