Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities

Creator/Principal investigator(s)

Thomas Kieselbach - Umeå University, Department of Chemistry orcid

Christiane Funk - Umeå University, Department of Chemistry

Beverley Green - University of British Columbia, Biological Sciences Building

Otilia Cheregi - University of Gothenburg, Department of Biological and Environmental Sciences

Description

Plants and algae have developed various light-harvesting mechanisms for optimal delivery of excitation energy to the photosystems. Cryptophyte algae have evolved a novel soluble light-harvesting antenna utilizing phycobilin pigments to complement the membrane-intrinsic Chl a/c-binding LHC antenna. This new antenna consists of the plastid-encoded β-subunit, a relic of the ancestral phycobilisome, and a novel nuclear-encoded α-subunit unique to cryptophytes. Together, these proteins form the active α1β·α2β-tetramer.
In all cryptophyte algae investigated so far, the α-subunits have duplicated and diversified into a large gene family. Although there is transcriptional evidence for expression of all these genes, the X-ray structures determined to date suggest that only two of the α-subunit genes might be significantly expressed at the protein level.
Using proteomics, we show that in phycoerythrin 545 (PE545) of Guillardia theta, the only cryptophyte with a sequenced genome, all 20 α-subunits are expressed when the algae grow under white light. The expression level of each protein depends on the i

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Responsible department/unit

Umeå University, Department of Chemistry

Creator/Principal investigator(s)

Thomas Kieselbach - Umeå University, Department of Chemistry orcid

Christiane Funk - Umeå University, Department of Chemistry

Beverley Green - University of British Columbia, Biological Sciences Building

Otilia Cheregi - University of Gothenburg, Department of Biological and Environmental Sciences

Identifiers

SND-ID: EXT 1130

DOI: https://doi.org/10.6019/PXD006301

Description

Plants and algae have developed various light-harvesting mechanisms for optimal delivery of excitation energy to the photosystems. Cryptophyte algae have evolved a novel soluble light-harvesting antenna utilizing phycobilin pigments to complement the membrane-intrinsic Chl a/c-binding LHC antenna. This new antenna consists of the plastid-encoded β-subunit, a relic of the ancestral phycobilisome, and a novel nuclear-encoded α-subunit unique to cryptophytes. Together, these proteins form the active α1β·α2β-tetramer.
In all cryptophyte algae investigated so far, the α-subunits have duplicated and diversified into a large gene family. Although there is transcriptional evidence for expression of all these genes, the X-ray structures determined to date suggest that only two of the α-subunit genes might be significantly expressed at the protein level.
Using proteomics, we show that in phycoerythrin 545 (PE545) of Guillardia theta, the only cryptophyte with a sequenced genome, all 20 α-subunits are expressed when the algae grow under white light. The expression level of each protein depends on the i

... Show more..

Language

English

Unit of analysis

Sampling procedure

Other

Funding

Artificial Leaf and Solar Fuel Project, KAW — Ref. KAW 2011-0055

Swedish Energi Agency — Ref. 2012-005889

Contact for questions about the data

Thomas Kieselbach

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Publications

Kieselbach T, Cheregi O, Green BR, Funk C. Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities. Photosynth Res. 2018 Mar;135(1-3):149-163. DOI:10.1007/s11120-017-0400-0
DOI: https://doi.org/10.1007/s11120-017-0400-0

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License

Creative Commons License

Phycobili antenna proteins of Guillarida theta

Creator/Principal investigator(s)

Thomas Kieselbach - Umeå University, Department of Chemistry orcid

Christiane Funk - Umeå University, Department of Chemistry

Beverley Green - University of British Columbia, Biological Sciences Building

Otilia Cheregi - University of Gothenburg, Department of Biological and Environmental Sciences

Description

The dataset contains all 45 raw data files from the mass spectrometry analysis (LC-MS/MS) of the cultures of the alga Guillardia theta, which were analyzed in this study. These files have Waters raw format and can be processed with commercial software such as ProteinLynx Global server 3.0 and Mascot Distiller 2.5. The algae, which were grown under optimal light, were analyzed in the NL-series. The algae, which were grown under high light intensity, were analyzed in the HL-series, and the algae,

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Data format / data structure

Text

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Published: 2019-11-25