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Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803

In cyanobacteria such as Synechocystis sp. PCC 6803, large antenna complexes called phycobilisomes (PBS) harvest light and transfer the energy to the photosynthetic reaction centers. Modification of the light harvesting machinery in cyanobacteria has widespread consequences, causing changes in cell...

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Autores principales: Liberton, Michelle, Chrisler, William B., Nicora, Carrie D., Moore, Ronald J., Smith, Richard D., Koppenaal, David W., Pakrasi, Himadri B., Jacobs, Jon M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333879/
https://www.ncbi.nlm.nih.gov/pubmed/28253354
http://dx.doi.org/10.1371/journal.pone.0173251
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author Liberton, Michelle
Chrisler, William B.
Nicora, Carrie D.
Moore, Ronald J.
Smith, Richard D.
Koppenaal, David W.
Pakrasi, Himadri B.
Jacobs, Jon M.
author_facet Liberton, Michelle
Chrisler, William B.
Nicora, Carrie D.
Moore, Ronald J.
Smith, Richard D.
Koppenaal, David W.
Pakrasi, Himadri B.
Jacobs, Jon M.
author_sort Liberton, Michelle
collection PubMed
description In cyanobacteria such as Synechocystis sp. PCC 6803, large antenna complexes called phycobilisomes (PBS) harvest light and transfer the energy to the photosynthetic reaction centers. Modification of the light harvesting machinery in cyanobacteria has widespread consequences, causing changes in cell morphology and physiology. In the current study, we investigated the effects of PBS truncation on the proteomes of three Synechocystis 6803 PBS antenna mutants. These range from the progressive truncation of phycocyanin rods in the CB and CK strains, to full removal of PBS in the PAL mutant. Comparative quantitative protein results revealed surprising changes in protein abundances in the mutant strains. Our results showed that PBS truncation in Synechocystis 6803 broadly impacted core cellular mechanisms beyond light harvesting and photosynthesis. Specifically, we observed dramatic alterations in membrane transport mechanisms, where the most severe PBS truncation in the PAL strain appeared to suppress the cellular utilization and regulation of bicarbonate and iron. These changes point to the role of PBS as a component critical to cell function, and demonstrate the continuing need to assess systems-wide protein based abundances to understand potential indirect phenotypic effects.
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spelling pubmed-53338792017-03-10 Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803 Liberton, Michelle Chrisler, William B. Nicora, Carrie D. Moore, Ronald J. Smith, Richard D. Koppenaal, David W. Pakrasi, Himadri B. Jacobs, Jon M. PLoS One Research Article In cyanobacteria such as Synechocystis sp. PCC 6803, large antenna complexes called phycobilisomes (PBS) harvest light and transfer the energy to the photosynthetic reaction centers. Modification of the light harvesting machinery in cyanobacteria has widespread consequences, causing changes in cell morphology and physiology. In the current study, we investigated the effects of PBS truncation on the proteomes of three Synechocystis 6803 PBS antenna mutants. These range from the progressive truncation of phycocyanin rods in the CB and CK strains, to full removal of PBS in the PAL mutant. Comparative quantitative protein results revealed surprising changes in protein abundances in the mutant strains. Our results showed that PBS truncation in Synechocystis 6803 broadly impacted core cellular mechanisms beyond light harvesting and photosynthesis. Specifically, we observed dramatic alterations in membrane transport mechanisms, where the most severe PBS truncation in the PAL strain appeared to suppress the cellular utilization and regulation of bicarbonate and iron. These changes point to the role of PBS as a component critical to cell function, and demonstrate the continuing need to assess systems-wide protein based abundances to understand potential indirect phenotypic effects. Public Library of Science 2017-03-02 /pmc/articles/PMC5333879/ /pubmed/28253354 http://dx.doi.org/10.1371/journal.pone.0173251 Text en © 2017 Liberton et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Liberton, Michelle
Chrisler, William B.
Nicora, Carrie D.
Moore, Ronald J.
Smith, Richard D.
Koppenaal, David W.
Pakrasi, Himadri B.
Jacobs, Jon M.
Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title_full Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title_fullStr Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title_full_unstemmed Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title_short Phycobilisome truncation causes widespread proteome changes in Synechocystis sp. PCC 6803
title_sort phycobilisome truncation causes widespread proteome changes in synechocystis sp. pcc 6803
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333879/
https://www.ncbi.nlm.nih.gov/pubmed/28253354
http://dx.doi.org/10.1371/journal.pone.0173251
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