Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.

In Arabidopsis thaliana, the Light-Oxygen-Voltage (LOV) domain containing protein ZEITLUPE (ZTL) integrates light quality, intensity, and duration into regulation of the circadian clock. Recent structural and biochemical studies of ZTL indicate that the protein diverges from other members of the LOV...

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Autores principales:	Francesco Trozzi, Feng Wang, Gennady Verkhivker, Brian D Zoltowski, Peng Tao
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/103680ec68754de2bfdd65f598f5b53f
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spelling	oai:doaj.org-article:103680ec68754de2bfdd65f598f5b53f2021-12-02T19:57:31ZDimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.1553-734X1553-735810.1371/journal.pcbi.1009168https://doaj.org/article/103680ec68754de2bfdd65f598f5b53f2021-07-01T00:00:00Zhttps://doi.org/10.1371/journal.pcbi.1009168https://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358In Arabidopsis thaliana, the Light-Oxygen-Voltage (LOV) domain containing protein ZEITLUPE (ZTL) integrates light quality, intensity, and duration into regulation of the circadian clock. Recent structural and biochemical studies of ZTL indicate that the protein diverges from other members of the LOV superfamily in its allosteric mechanism, and that the divergent allosteric mechanism hinges upon conservation of two signaling residues G46 and V48 that alter dynamic motions of a Gln residue implicated in signal transduction in all LOV proteins. Here, we delineate the allosteric mechanism of ZTL via an integrated computational approach that employs atomistic simulations of wild type and allosteric variants of ZTL in the functional dark and light states, together with Markov state and supervised machine learning classification models. This approach has unveiled key factors of the ZTL allosteric mechanisms, and identified specific interactions and residues implicated in functional allosteric changes. The final results reveal atomic level insights into allosteric mechanisms of ZTL function that operate via a non-trivial combination of population-shift and dynamics-driven allosteric pathways.Francesco TrozziFeng WangGennady VerkhivkerBrian D ZoltowskiPeng TaoPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 17, Iss 7, p e1009168 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Francesco Trozzi Feng Wang Gennady Verkhivker Brian D Zoltowski Peng Tao Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
description	In Arabidopsis thaliana, the Light-Oxygen-Voltage (LOV) domain containing protein ZEITLUPE (ZTL) integrates light quality, intensity, and duration into regulation of the circadian clock. Recent structural and biochemical studies of ZTL indicate that the protein diverges from other members of the LOV superfamily in its allosteric mechanism, and that the divergent allosteric mechanism hinges upon conservation of two signaling residues G46 and V48 that alter dynamic motions of a Gln residue implicated in signal transduction in all LOV proteins. Here, we delineate the allosteric mechanism of ZTL via an integrated computational approach that employs atomistic simulations of wild type and allosteric variants of ZTL in the functional dark and light states, together with Markov state and supervised machine learning classification models. This approach has unveiled key factors of the ZTL allosteric mechanisms, and identified specific interactions and residues implicated in functional allosteric changes. The final results reveal atomic level insights into allosteric mechanisms of ZTL function that operate via a non-trivial combination of population-shift and dynamics-driven allosteric pathways.
format	article
author	Francesco Trozzi Feng Wang Gennady Verkhivker Brian D Zoltowski Peng Tao
author_facet	Francesco Trozzi Feng Wang Gennady Verkhivker Brian D Zoltowski Peng Tao
author_sort	Francesco Trozzi
title	Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
title_short	Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
title_full	Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
title_fullStr	Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
title_full_unstemmed	Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.
title_sort	dimeric allostery mechanism of the plant circadian clock photoreceptor zeitlupe.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/103680ec68754de2bfdd65f598f5b53f
work_keys_str_mv	AT francescotrozzi dimericallosterymechanismoftheplantcircadianclockphotoreceptorzeitlupe AT fengwang dimericallosterymechanismoftheplantcircadianclockphotoreceptorzeitlupe AT gennadyverkhivker dimericallosterymechanismoftheplantcircadianclockphotoreceptorzeitlupe AT briandzoltowski dimericallosterymechanismoftheplantcircadianclockphotoreceptorzeitlupe AT pengtao dimericallosterymechanismoftheplantcircadianclockphotoreceptorzeitlupe
_version_	1718375824731668480

Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.

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