Red light-induced structure changes in phytochrome A from Pisum sativum

Abstract Phytochrome A (phyA) is a photoreceptor protein of plants that regulates the red/far-red light photomorphogenic responses of plants essential for growth and development. PhyA, composed of approximately 1100 amino acid residues, folds into photosensory and output signaling modules. The photo...

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Autores principales: Mao Oide, Masayoshi Nakasako
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/2932b6c2340e44cfbc116dded6222021
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spelling oai:doaj.org-article:2932b6c2340e44cfbc116dded62220212021-12-02T14:06:19ZRed light-induced structure changes in phytochrome A from Pisum sativum10.1038/s41598-021-82544-22045-2322https://doaj.org/article/2932b6c2340e44cfbc116dded62220212021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82544-2https://doaj.org/toc/2045-2322Abstract Phytochrome A (phyA) is a photoreceptor protein of plants that regulates the red/far-red light photomorphogenic responses of plants essential for growth and development. PhyA, composed of approximately 1100 amino acid residues, folds into photosensory and output signaling modules. The photosensory module covalently binds phytochromobilin as a chromophore for photoreversible interconversion between inactive red light-absorbing (Pr) and active far-red light-absorbing (Pfr) forms to act as a light-driven phosphorylation enzyme. To understand the molecular mechanism in the initial process of photomorphogenic response, we studied the molecular structures of large phyA (LphyA) from Pisum sativum, which lacks the 52 residues in the N-terminal, by small-angle X-ray scattering combined with multivariate analyses applied to molecular models predicted from the scattering profiles. According to our analyses, Pr was in a dimer and had a four-leaf shape, and the subunit was approximated as a bent rod of 175 × 50 Å. The scattering profile of Pfr was calculated from that recorded for a mixture of Pr and Pfr under red-light irradiation by using their population determined from the absorption spectrum. The Pfr dimer exhibited a butterfly shape composed of subunits with a straight rod of 175 × 50 Å. The shape differences between Pr and Pfr indicated conformational changes in the Pr/Pfr interconversion which would be essential to the interaction with protein molecules involved in transcriptional control.Mao OideMasayoshi NakasakoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Mao Oide
Masayoshi Nakasako
Red light-induced structure changes in phytochrome A from Pisum sativum
description Abstract Phytochrome A (phyA) is a photoreceptor protein of plants that regulates the red/far-red light photomorphogenic responses of plants essential for growth and development. PhyA, composed of approximately 1100 amino acid residues, folds into photosensory and output signaling modules. The photosensory module covalently binds phytochromobilin as a chromophore for photoreversible interconversion between inactive red light-absorbing (Pr) and active far-red light-absorbing (Pfr) forms to act as a light-driven phosphorylation enzyme. To understand the molecular mechanism in the initial process of photomorphogenic response, we studied the molecular structures of large phyA (LphyA) from Pisum sativum, which lacks the 52 residues in the N-terminal, by small-angle X-ray scattering combined with multivariate analyses applied to molecular models predicted from the scattering profiles. According to our analyses, Pr was in a dimer and had a four-leaf shape, and the subunit was approximated as a bent rod of 175 × 50 Å. The scattering profile of Pfr was calculated from that recorded for a mixture of Pr and Pfr under red-light irradiation by using their population determined from the absorption spectrum. The Pfr dimer exhibited a butterfly shape composed of subunits with a straight rod of 175 × 50 Å. The shape differences between Pr and Pfr indicated conformational changes in the Pr/Pfr interconversion which would be essential to the interaction with protein molecules involved in transcriptional control.
format article
author Mao Oide
Masayoshi Nakasako
author_facet Mao Oide
Masayoshi Nakasako
author_sort Mao Oide
title Red light-induced structure changes in phytochrome A from Pisum sativum
title_short Red light-induced structure changes in phytochrome A from Pisum sativum
title_full Red light-induced structure changes in phytochrome A from Pisum sativum
title_fullStr Red light-induced structure changes in phytochrome A from Pisum sativum
title_full_unstemmed Red light-induced structure changes in phytochrome A from Pisum sativum
title_sort red light-induced structure changes in phytochrome a from pisum sativum
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/2932b6c2340e44cfbc116dded6222021
work_keys_str_mv AT maooide redlightinducedstructurechangesinphytochromeafrompisumsativum
AT masayoshinakasako redlightinducedstructurechangesinphytochromeafrompisumsativum
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