@article {Demory2017,
	title = {Temperature is a key factor in Micromonas{\textendash}virus interactions},
	journal = {The ISME Journal},
	volume = {11},
	number = {3},
	year = {2017},
	note = {Publisher: Nature Publishing Group tex.mendeley-tags: 2017,RCC4229,RCC4253,RCC4265,RCC451,RCC829,RCC834,sbr?hyto$_\textrmd$ipo,sbr?hyto?app},
	month = {mar},
	pages = {601{\textendash}612},
	abstract = {The genus Micromonas comprises phytoplankton that show among the widest latitudinal distributions on Earth, and members of this genus are recurrently infected by prasinoviruses in contrasted thermal ecosystems. In this study, we assessed how temperature influences the interplay between the main genetic clades of this prominent microalga and their viruses. The growth of three Micromonas strains (Mic-A, Mic-B, Mic-C) and the stability of their respective lytic viruses (MicV-A, MicV-B, MicV-C) were measured over a thermal range of 4{\textendash}32.5 {\textdegree}C. Similar growth temperature optima (Topt) were predicted for all three hosts but Mic-B exhibited a broader thermal tolerance than Mic-A and Mic-C, suggesting distinct thermoacclimation strategies. Similarly, the MicV-C virus displayed a remarkable thermal stability compared with MicV-A and MicV-B. Despite these divergences, infection dynamics showed that temperatures below Topt lengthened lytic cycle kinetics and reduced viral yield and, notably, that infection at temperatures above Topt did not usually result in cell lysis. Two mechanisms operated depending on the temperature and the biological system. Hosts either prevented the production of viral progeny or maintained their ability to produce virions with no apparent cell lysis, pointing to a possible switch in the viral life strategy. Hence, temperature changes critically affect the outcome of Micromonas infection and have implications for ocean biogeochemistry and evolution.},
	keywords = {2017, RCC4229, RCC4253, RCC4265, RCC451, RCC829, RCC834, sbr?hyto$_\textrmd$ipo, sbr?hyto?app},
	issn = {1751-7362},
	doi = {10.1038/ismej.2016.160},
	url = {http://dx.doi.org/10.1038/ismej.2016.160 http://www.nature.com/doifinder/10.1038/ismej.2016.160},
	author = {Demory, David and Arsenieff, Laure and Simon, Nathalie and Six, Christophe and Rigaut-jalabert, Fabienne and Marie, Dominique and Ge, Pei and Bigeard, Estelle and Jacquet, St{\'e}phan and Sciandra, Antoine and Bernard, Olivier and Rabouille, Sophie and Baudoux, Anne-claire}
}
@article {Six2005,
	title = {Two novel phycoerythrin-associated linker proteins in the marine cyanobacterium synechococcus sp. Strain WH8102},
	journal = {Journal of Bacteriology},
	volume = {187},
	number = {5},
	year = {2005},
	note = {tex.mendeley-tags: 2005,rcc,sbr?hyto},
	pages = {1685{\textendash}1694},
	abstract = {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 beta 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.},
	keywords = {2005, rcc, SBR$_\textrmP$hyto, sbr?hyto},
	doi = {10.1128/JB.187.5.1685-1694.2005},
	url = {http://jb.asm.org/cgi/content/abstract/187/5/1685},
	author = {Six, Christophe and Thomas, Jean-Claude and Thion, Laurent and Lemoine, Yves and Zal, Frank and Partensky, Fr{\'e}d{\'e}ric}
}
