Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1

Abstract Light-Oxygen-Voltage (LOV) domains are responsible for detecting blue light (BL) and regulating the activities of effector domains in various organisms. Photozipper (PZ), an N-terminally truncated aureochrome-1 protein, contains a LOV domain and a basic leucin zipper (bZIP) domain and plays...

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Autores principales:	Hiroto Nakajima, Itsuki Kobayashi, Yumiko Adachi, Osamu Hisatomi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f9119fdc81cd4c7eb6551e769074540b
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spelling	oai:doaj.org-article:f9119fdc81cd4c7eb6551e769074540b2021-12-02T17:34:49ZTransmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-110.1038/s41598-021-91497-52045-2322https://doaj.org/article/f9119fdc81cd4c7eb6551e769074540b2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91497-5https://doaj.org/toc/2045-2322Abstract Light-Oxygen-Voltage (LOV) domains are responsible for detecting blue light (BL) and regulating the activities of effector domains in various organisms. Photozipper (PZ), an N-terminally truncated aureochrome-1 protein, contains a LOV domain and a basic leucin zipper (bZIP) domain and plays a role as a light-activatable transcription factor. PZ is monomeric in the dark state and undergoes non-covalent dimerization upon illumination with BL, subsequently increasing its affinity for the target DNA. To clarify the molecular mechanism of aureochromes, we prepared site-directed mutants of PZ and performed quantitative analyses in the dark and light states. Although the amino acid substitutions in the hinge region between the LOV core and A’α helix had minor effects on the dimerization and DNA-binding properties of PZ, the substitutions in the β-sheet region of the LOV core and in the A’α helix significantly affected these properties. We found that light signals are transmitted from the LOV core to the effector bZIP domain via the hydrophobic residues on the β-sheet. The light-induced conformational change possibly deforms the hydrophobic regions of the LOV core and induces the detachment of the A’α helix to expose the dimerization surface, likely activating the bZIP domain in a light-dependent manner.Hiroto NakajimaItsuki KobayashiYumiko AdachiOsamu HisatomiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hiroto Nakajima Itsuki Kobayashi Yumiko Adachi Osamu Hisatomi Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
description	Abstract Light-Oxygen-Voltage (LOV) domains are responsible for detecting blue light (BL) and regulating the activities of effector domains in various organisms. Photozipper (PZ), an N-terminally truncated aureochrome-1 protein, contains a LOV domain and a basic leucin zipper (bZIP) domain and plays a role as a light-activatable transcription factor. PZ is monomeric in the dark state and undergoes non-covalent dimerization upon illumination with BL, subsequently increasing its affinity for the target DNA. To clarify the molecular mechanism of aureochromes, we prepared site-directed mutants of PZ and performed quantitative analyses in the dark and light states. Although the amino acid substitutions in the hinge region between the LOV core and A’α helix had minor effects on the dimerization and DNA-binding properties of PZ, the substitutions in the β-sheet region of the LOV core and in the A’α helix significantly affected these properties. We found that light signals are transmitted from the LOV core to the effector bZIP domain via the hydrophobic residues on the β-sheet. The light-induced conformational change possibly deforms the hydrophobic regions of the LOV core and induces the detachment of the A’α helix to expose the dimerization surface, likely activating the bZIP domain in a light-dependent manner.
format	article
author	Hiroto Nakajima Itsuki Kobayashi Yumiko Adachi Osamu Hisatomi
author_facet	Hiroto Nakajima Itsuki Kobayashi Yumiko Adachi Osamu Hisatomi
author_sort	Hiroto Nakajima
title	Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
title_short	Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
title_full	Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
title_fullStr	Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
title_full_unstemmed	Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
title_sort	transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f9119fdc81cd4c7eb6551e769074540b
work_keys_str_mv	AT hirotonakajima transmissionoflightsignalsfromthelightoxygenvoltagecoreviathehydrophobicregionofthebsheetsurfaceinaureochrome1 AT itsukikobayashi transmissionoflightsignalsfromthelightoxygenvoltagecoreviathehydrophobicregionofthebsheetsurfaceinaureochrome1 AT yumikoadachi transmissionoflightsignalsfromthelightoxygenvoltagecoreviathehydrophobicregionofthebsheetsurfaceinaureochrome1 AT osamuhisatomi transmissionoflightsignalsfromthelightoxygenvoltagecoreviathehydrophobicregionofthebsheetsurfaceinaureochrome1
_version_	1718379976589312000

Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1

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