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Journal of Bacteriology, March 2005, p. 1685-1694, Vol. 187, No. 5
0021-9193/05/$08.00+0     doi:10.1128/JB.187.5.1685-1694.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Two Novel Phycoerythrin-Associated Linker Proteins in the Marine Cyanobacterium Synechococcus sp. Strain WH8102

Christophe Six,1,{dagger} Jean-Claude Thomas,2,{dagger} Laurent Thion,1 Yves Lemoine,3 Frank Zal,1 and Frédéric Partensky1*

Département "Phytoplancton Océanique," Station Biologique, UMR 7127 CNRS, and Université Pierre et Marie Curie, Roscoff,1 Département "Organismes Photosynthétiques et Environnement," FRE 2433, CNRS, and Ecole Normale Supérieure, Paris,2 Département "Phycologie et Production primaire," UMR 8013 CNRS, and Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France3

Received 17 August 2004/ Accepted 30 November 2004

The recent availability of the whole genome of Synechococcus sp. strain WH8102 allows us to have a global view of the complex structure of the phycobilisomes of this marine picocyanobacterium. Genomic analyses revealed several new characteristics of these phycobilisomes, consisting of an allophycocyanin core and rods made of one type of phycocyanin and two types of phycoerythrins (I and II). Although the allophycocyanin appears to be similar to that found commonly in freshwater cyanobacteria, the phycocyanin is simpler since it possesses only one complete set of {alpha} and ß subunits and two rod-core linkers (CpcG1 and CpcG2). It is therefore probably made of a single hexameric disk per rod. In contrast, we have found two novel putative phycoerythrin-associated linker polypeptides that appear to be specific for marine Synechococcus spp. The first one (SYNW2000) is unusually long (548 residues) and apparently results from the fusion of a paralog of MpeC, a phycoerythrin II linker, and of CpeD, a phycoerythrin-I linker. The second one (SYNW1989) has a more classical size (300 residues) and is also an MpeC paralog. A biochemical analysis revealed that, like MpeC, these two novel linkers were both chromophorylated with phycourobilin. Our data suggest that they are both associated (partly or totally) with phycoerythrin II, and we propose to name SYNW2000 and SYNW1989 MpeD and MpeE, respectively. We further show that acclimation of phycobilisomes to high light leads to a dramatic reduction of MpeC, whereas the two novel linkers are not significantly affected. Models for the organization of the rods are proposed.

* Corresponding author. Mailing address: Station Biologique, UMR 7127 CNRS & Université Pierre et Marie Curie, BP 74, 29682 Roscoff cedex, France. Phone: 33-298-29-2314. Fax: 33-298-29-2324. E-mail: partensky{at}sb-roscoff.fr.

{dagger} C.S. and J.-C.T. contributed equally to the work.

Journal of Bacteriology, March 2005, p. 1685-1694, Vol. 187, No. 5
0021-9193/05/$08.00+0     doi:10.1128/JB.187.5.1685-1694.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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