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Proteomic analysis ...
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Kieselbach, ThomasUmeå universitet,Kemiska institutionen
(författare)
Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities
- Artikel/kapitelEngelska2018
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2017-05-24
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Springer,2018
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electronicrdacarrier
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LIBRIS-ID:oai:DiVA.org:umu-143747
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-143747URI
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https://doi.org/10.1007/s11120-017-0400-0DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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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.
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Biuppslag (personer, institutioner, konferenser, titlar ...)
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Cheregi, OtiliaUmeå universitet,Kemiska institutionen(Swepub:umu)otch0001
(författare)
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Green, Beverley R.
(författare)
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Funk, ChristianeUmeå universitet,Kemiska institutionen(Swepub:umu)chefuk04
(författare)
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Umeå universitetKemiska institutionen
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Photosynthesis Research: Springer135:1–3, s. 149-1630166-85951573-5079
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