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

This data description has been automatically migrated from Umeå University, Department of Chemistry to SND’s research data catalogue. The level of documentation may therefore differ from other data descriptions in the catalogue.

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: 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:

Swedish Energi Agency — Ref. 2012-005889

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

Contact for questions about the data:

Thomas Kieselbach

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Publications

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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

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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