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Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae
[Image: see text] Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly acting to absorb light where chlorophyll cannot (500–650 nm), phycobiliproteins also play an instrumental role in help...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8949638/ https://www.ncbi.nlm.nih.gov/pubmed/35350600 http://dx.doi.org/10.1021/acscentsci.1c01209 |
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author | Spangler, Leah C. Yu, Mina Jeffrey, Philip D. Scholes, Gregory D. |
author_facet | Spangler, Leah C. Yu, Mina Jeffrey, Philip D. Scholes, Gregory D. |
author_sort | Spangler, Leah C. |
collection | PubMed |
description | [Image: see text] Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly acting to absorb light where chlorophyll cannot (500–650 nm), phycobiliproteins also play an instrumental role in helping cryptophyte algae respond to changes in light intensity through the process of photoacclimation. Until recently, photoacclimation in cryptophyte algae was only observed as a change in the cellular concentration of phycobiliproteins; however, an additional photoacclimation response was recently discovered that causes shifts in the phycobiliprotein absorbance peaks following growth under red, blue, or green light. Here, we reproduce this newly identified photoacclimation response in two species of cryptophyte algae and elucidate the origin of the response on the protein level. We compare isolated native and photoacclimated phycobiliproteins for these two species using spectroscopy and mass spectrometry, and we report the X-ray structures of each phycobiliprotein and the corresponding photoacclimated complex. We find that neither the protein sequences nor the protein structures are modified by photoacclimation. We conclude that cryptophyte algae change one chromophore in the phycobiliprotein β subunits in response to changes in the spectral quality of light. Ultrafast pump–probe spectroscopy shows that the energy transfer is weakly affected by photoacclimation. |
format | Online Article Text |
id | pubmed-8949638 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-89496382022-03-28 Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae Spangler, Leah C. Yu, Mina Jeffrey, Philip D. Scholes, Gregory D. ACS Cent Sci [Image: see text] Cryptophyte algae are well-known for their ability to survive under low light conditions using their auxiliary light harvesting antennas, phycobiliproteins. Mainly acting to absorb light where chlorophyll cannot (500–650 nm), phycobiliproteins also play an instrumental role in helping cryptophyte algae respond to changes in light intensity through the process of photoacclimation. Until recently, photoacclimation in cryptophyte algae was only observed as a change in the cellular concentration of phycobiliproteins; however, an additional photoacclimation response was recently discovered that causes shifts in the phycobiliprotein absorbance peaks following growth under red, blue, or green light. Here, we reproduce this newly identified photoacclimation response in two species of cryptophyte algae and elucidate the origin of the response on the protein level. We compare isolated native and photoacclimated phycobiliproteins for these two species using spectroscopy and mass spectrometry, and we report the X-ray structures of each phycobiliprotein and the corresponding photoacclimated complex. We find that neither the protein sequences nor the protein structures are modified by photoacclimation. We conclude that cryptophyte algae change one chromophore in the phycobiliprotein β subunits in response to changes in the spectral quality of light. Ultrafast pump–probe spectroscopy shows that the energy transfer is weakly affected by photoacclimation. American Chemical Society 2022-02-09 2022-03-23 /pmc/articles/PMC8949638/ /pubmed/35350600 http://dx.doi.org/10.1021/acscentsci.1c01209 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Spangler, Leah C. Yu, Mina Jeffrey, Philip D. Scholes, Gregory D. Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae |
title | Controllable Phycobilin Modification: An Alternative
Photoacclimation Response in Cryptophyte Algae |
title_full | Controllable Phycobilin Modification: An Alternative
Photoacclimation Response in Cryptophyte Algae |
title_fullStr | Controllable Phycobilin Modification: An Alternative
Photoacclimation Response in Cryptophyte Algae |
title_full_unstemmed | Controllable Phycobilin Modification: An Alternative
Photoacclimation Response in Cryptophyte Algae |
title_short | Controllable Phycobilin Modification: An Alternative
Photoacclimation Response in Cryptophyte Algae |
title_sort | controllable phycobilin modification: an alternative
photoacclimation response in cryptophyte algae |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8949638/ https://www.ncbi.nlm.nih.gov/pubmed/35350600 http://dx.doi.org/10.1021/acscentsci.1c01209 |
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