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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03655naa a2200433 4500 | |
| 001 | oai:DiVA.org:umu-143747 | |
| 003 | SwePub | |
| 008 | 180108s2018 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1437472 URI |
| 024 | 7 | a https://doi.org/10.1007/s11120-017-0400-02 DOI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Kieselbach, Thomasu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)thskih04 |
| 245 | 1 0 | a Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities |
| 264 | c 2017-05-24 | |
| 264 | 1 | b Springer,c 2018 |
| 338 | a electronic2 rdacarrier | |
| 520 | a 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. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a Cryptophyta | |
| 653 | a Phycobilin | |
| 653 | a Phycobiliprotein | |
| 653 | a Translation | |
| 653 | a TAT-pathway | |
| 653 | a Proteomics | |
| 700 | 1 | a Cheregi, Otiliau Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)otch0001 |
| 700 | 1 | a Green, Beverley R.4 aut |
| 700 | 1 | a Funk, Christianeu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)chefuk04 |
| 710 | 2 | a Umeå universitetb Kemiska institutionen4 org |
| 773 | 0 | t Photosynthesis Researchd : Springerg 135:1–3, s. 149-163q 135:1–3<149-163x 0166-8595x 1573-5079 |
| 856 | 4 | u https://doi.org/10.1007/s11120-017-0400-0y Fulltext |
| 856 | 4 | u https://umu.diva-portal.org/smash/get/diva2:1171620/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print |
| 856 | 4 | u https://link.springer.com/content/pdf/10.1007%2Fs11120-017-0400-0.pdf |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-143747 |
| 856 | 4 8 | u https://doi.org/10.1007/s11120-017-0400-0 |
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