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The small CAB-like proteins of Synechocystis sp. PCC 6803 bind chlorophyll: In vitro pigment reconstitution studies on one-helix light-harvesting-like proteins.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
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2008 (English)In: Photosynthesis Research, ISSN 0166-8595, Vol. 98, no 1/3, 479-488 p.Article in journal (Refereed) Published
Abstract [en]

The large family of light-harvesting-like proteins contains members with one to four membrane spanning helices with significant homology to the chlorophyll a/b-binding antenna proteins of plants. From structural as well as evolutionary perspective, it is likely that the members of this family bind chlorophylls and carotenoids. However, undisputable evidence is still lacking. The cyanobacterial small CAB-like proteins (SCPs) are one-helix proteins with compelling similarity to the first and third transmembrane helix of LHCII (LHCIIb) including the chlorophyll-binding motifs. They have been proposed to act as chlorophyll-carrier proteins. Here, we analyze the in vivo absorption spectra of single scp deletion mutants in Synechocystis sp. PCC 6803 and compare the in vitro pigment binding ability of the SCP pairs ScpC/D and ScpB/E with the one of LHCII and a synthetic peptide containing the chlorophyll-binding motif (Eggink LL, Hoober JK (2000) J Biol Chem 275:9087–9090). We demonstrate that deletion of scpB alters the pigmentation in the cyanobacterial cell. Furthermore, we are able to show that chlorophylls and carotenoids interact in vitro with the pairs of ScpC/D and ScpB/E, demonstrated by fluorescence resonance energy transfer and circular dichroism.

Place, publisher, year, edition, pages
SpringerLink , 2008. Vol. 98, no 1/3, 479-488 p.
Keyword [en]
Antenna, Chlorophyll-binding protein, Cyanobacteria, Early-light-induced proteins (ELIPs), High-light-induced proteins (HLIPs), Light-harvesting complex, Synechocystis sp. PCC 6803
URN: urn:nbn:se:umu:diva-10636DOI: 10.1007/s11120-008-9368-0PubMedID: 18836846OAI: diva2:150307
Available from: 2008-12-11 Created: 2008-12-11 Last updated: 2009-09-10Bibliographically approved
In thesis
1. The Small Cab-like Proteins in the cyanobacterium Synechocystis sp. PCC 6803
Open this publication in new window or tab >>The Small Cab-like Proteins in the cyanobacterium Synechocystis sp. PCC 6803
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The Small Cab-like Proteins (SCPs) in the cyanobacterium Synechocystis sp. PCC 6803 accumulate in cells grown under different stress conditions. Genes coding for SCPs have been found in all sequenced organisms performing oxygenic photosynthesis and even in the genomes of cyanophages. Deletion of multiple scp genes in Synechocystis resulted in mutants with severely impaired growth and altered pigment content. These findings indicate the importance of SCPs in photosynthesis; however, their specific function is not well understood. SCPs share a chlorophyll-binding motif with the plant light harvesting complex, suggesting that they bind chlorophyll. Here I describe my findings, which unambiguously show that SCPs are able to bind chlorophyll in vitro. Although they affect both the stoichiometric ratio of Photosystem I to II and chlorophyll stability, they do not seem to be directly involved in non-photochemical quenching. I was able to reveal the location of the SCPs within the cyanobacterial cell: in stressed cells they attach to Photosystem II in the thylakoid membrane. Furthermore, I revealed the presence of another light-harvesting like (Lil)/SCP protein in Synechocystis sp. PCC 6803. The gene, slr1544, codifying for this newly characterised LilA protein, co-transcribes together with scpD and also appears to bind to Photosystem II during stress.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2009. 49 p.
Photosynthesis, Photosystem II, chlorophyll-binding proteins, tetrapyrrole biosynthesis, photodamage, non-photochemical quenching, SCPs, LHCII
National Category
Biochemistry and Molecular Biology Botany
Research subject
urn:nbn:se:umu:diva-25886 (URN)978-91-7264-849-4 (ISBN)
Kemi, 90187, Umeå
Public defence
2009-10-02, KB3B9, KBChuset, Umeå Universitet, Umeå, 13:00 (English)
Available from: 2009-09-11 Created: 2009-09-09 Last updated: 2009-09-11Bibliographically approved

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