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- Kieselbach, ThomasUmeå universitet,Kemiska institutionen (author)
Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities
- Article/chapterEnglish2018
Publisher, publication year, extent ...
- 2017-05-24
- Springer,2018
- electronicrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:umu-143747
- https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-143747URI
- https://doi.org/10.1007/s11120-017-0400-0DOI
Supplementary language notes
- Language:English
- Summary in:English
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- SwePubSwePub
Classification
Notes
- 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 intensity of the growth light, but there is no evidence for a specific light-dependent regulation of individual members of the α-subunit family under the growth conditions applied. GtcpeA10 seems to be a special member of the α-subunit family, because it consists of two similar N- and C-terminal domains, which likely are the result of a partial tandem gene duplication. The proteomics data of this study have been deposited to the ProteomeXchange Consortium and have the dataset identifiers PXD006301 and 10.6019/PXD006301.
Subject headings and genre
- NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
- Cryptophyta
- Phycobilin
- Phycobiliprotein
- Translation
- TAT-pathway
- Proteomics
Added entries (persons, corporate bodies, meetings, titles ...)
- Cheregi, OtiliaUmeå universitet,Kemiska institutionen(Swepub:umu)otch0001 (author)
- Green, Beverley R. (author)
- Funk, ChristianeUmeå universitet,Kemiska institutionen(Swepub:umu)chefuk04 (author)
- Umeå universitetKemiska institutionen (creator_code:org_t)
Related titles
- In:Photosynthesis Research: Springer135:1–3, s. 149-1630166-85951573-5079
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