The structure of photosystem I from a high-light-tolerant cyanobacteria

Photosynthetic organisms have adapted to survive a myriad of extreme environments from the earth’s deserts to its poles, yet the proteins that carry out the light reactions of photosynthesis are highly conserved from the cyanobacteria to modern day crops. To investigate adaptations of the photosynth...

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Autores principales:	Zachary Dobson, Safa Ahad, Jackson Vanlandingham, Hila Toporik, Natalie Vaughn, Michael Vaughn, Dewight Williams, Michael Reppert, Petra Fromme, Yuval Mazor
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	cyanobacterium aponinum cyanobacteria extermophile photosynthesis light reactions photosystems Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6f0a8fe46ec842df9ba2b2f4de6e3c8d
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spelling	oai:doaj.org-article:6f0a8fe46ec842df9ba2b2f4de6e3c8d2021-11-16T14:18:21ZThe structure of photosystem I from a high-light-tolerant cyanobacteria10.7554/eLife.675182050-084Xe67518https://doaj.org/article/6f0a8fe46ec842df9ba2b2f4de6e3c8d2021-08-01T00:00:00Zhttps://elifesciences.org/articles/67518https://doaj.org/toc/2050-084XPhotosynthetic organisms have adapted to survive a myriad of extreme environments from the earth’s deserts to its poles, yet the proteins that carry out the light reactions of photosynthesis are highly conserved from the cyanobacteria to modern day crops. To investigate adaptations of the photosynthetic machinery in cyanobacteria to excessive light stress, we isolated a new strain of cyanobacteria, Cyanobacterium aponinum 0216, from the extreme light environment of the Sonoran Desert. Here we report the biochemical characterization and the 2.7 Å resolution structure of trimeric photosystem I from this high-light-tolerant cyanobacterium. The structure shows a new conformation of the PsaL C-terminus that supports trimer formation of cyanobacterial photosystem I. The spectroscopic analysis of this photosystem I revealed a decrease in far-red absorption, which is attributed to a decrease in the number of long- wavelength chlorophylls. Using these findings, we constructed two chimeric PSIs in Synechocystis sp. PCC 6803 demonstrating how unique structural features in photosynthetic complexes can change spectroscopic properties, allowing organisms to thrive under different environmental stresses.Zachary DobsonSafa AhadJackson VanlandinghamHila ToporikNatalie VaughnMichael VaughnDewight WilliamsMichael ReppertPetra FrommeYuval MazoreLife Sciences Publications Ltdarticlecyanobacterium aponinumcyanobacteriaextermophilephotosynthesislight reactionsphotosystemsMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	cyanobacterium aponinum cyanobacteria extermophile photosynthesis light reactions photosystems Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	cyanobacterium aponinum cyanobacteria extermophile photosynthesis light reactions photosystems Medicine R Science Q Biology (General) QH301-705.5 Zachary Dobson Safa Ahad Jackson Vanlandingham Hila Toporik Natalie Vaughn Michael Vaughn Dewight Williams Michael Reppert Petra Fromme Yuval Mazor The structure of photosystem I from a high-light-tolerant cyanobacteria
description	Photosynthetic organisms have adapted to survive a myriad of extreme environments from the earth’s deserts to its poles, yet the proteins that carry out the light reactions of photosynthesis are highly conserved from the cyanobacteria to modern day crops. To investigate adaptations of the photosynthetic machinery in cyanobacteria to excessive light stress, we isolated a new strain of cyanobacteria, Cyanobacterium aponinum 0216, from the extreme light environment of the Sonoran Desert. Here we report the biochemical characterization and the 2.7 Å resolution structure of trimeric photosystem I from this high-light-tolerant cyanobacterium. The structure shows a new conformation of the PsaL C-terminus that supports trimer formation of cyanobacterial photosystem I. The spectroscopic analysis of this photosystem I revealed a decrease in far-red absorption, which is attributed to a decrease in the number of long- wavelength chlorophylls. Using these findings, we constructed two chimeric PSIs in Synechocystis sp. PCC 6803 demonstrating how unique structural features in photosynthetic complexes can change spectroscopic properties, allowing organisms to thrive under different environmental stresses.
format	article
author	Zachary Dobson Safa Ahad Jackson Vanlandingham Hila Toporik Natalie Vaughn Michael Vaughn Dewight Williams Michael Reppert Petra Fromme Yuval Mazor
author_facet	Zachary Dobson Safa Ahad Jackson Vanlandingham Hila Toporik Natalie Vaughn Michael Vaughn Dewight Williams Michael Reppert Petra Fromme Yuval Mazor
author_sort	Zachary Dobson
title	The structure of photosystem I from a high-light-tolerant cyanobacteria
title_short	The structure of photosystem I from a high-light-tolerant cyanobacteria
title_full	The structure of photosystem I from a high-light-tolerant cyanobacteria
title_fullStr	The structure of photosystem I from a high-light-tolerant cyanobacteria
title_full_unstemmed	The structure of photosystem I from a high-light-tolerant cyanobacteria
title_sort	structure of photosystem i from a high-light-tolerant cyanobacteria
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/6f0a8fe46ec842df9ba2b2f4de6e3c8d
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The structure of photosystem I from a high-light-tolerant cyanobacteria

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