The observation of only one FGE being active in case of sulfated polysaccharides raises the question of see more how sulfatases expressed under reference conditions are maturated or whether they are active at all. A recently described alternative model of sulfatase maturation was found by knocking out known maturation systems in E. coli ( Benjdia et al., 2007). Analogous knock out experiments would allow conclusions regarding alternative maturation systems in R. baltica SH1T. Since genetic tools for planctomycetes have been proven to be viable ( Jogler et al., 2011), respective experiments should be possible in the near future. Characteristic sulfatase expression

profiles were yielded relating to all substrates. In case of glucose, eight sulfatase genes were expressed, four arylsulfatases (RB4815, RB7875, RB3849, RB9091, RB9549) and four N-acetylgalactosamine-6 sulfate sulfatases (RB200, RB3403, RB198, RB9091). In previous transcriptome studies conducted by Wecker and colleagues, focusing on the life cycle of R. baltica SH1T and potential stress responses, selleck chemicals glucose also was the substrate of choice ( Wecker et al., 2009 and Wecker et al., 2010). Comparing

sulfatase expression data from those studies with this study, revealed a rather small intersect of two commonly expressed sulfatases, RB3403 and RB4815. RB3403 was observed by Wecker and co-workers to be repressed 300 min after heat shock induction. It was concluded, that RB3403 may be involved in morphological remodeling in response to heat stress. Possibly it is involved in restructuring

or adapting the holdfast substance that R. baltica SH1T is known for. RB4815 was hypothesized to be involved in attaching to solid surfaces, thus being part of the machinery enabling a sessile lifestyle. Though six sulfatases were expressed in the case of fucoidan, respective data are not considered since hardly any growth was seen for this substrate. The sulfatase expression profile from λ-carrageenan was observed to be comparable similar to that from the glucose with few exceptions. Two sulfatases that were active in the case of glucose (RB198, RB9549), were inactive in λ-carrageenan, instead two sulfatases were expressed, of which one (RB4787) was exclusively expressed in λ-carrageenan Unoprostone grown cells. Referring to chondroitin sulfate as substrate, 14 sulfatases were shown to be active, two N-acetylgalactosamine-6 sulfate sulfatases (RB406, RB9091) with one (RB9091) being upregulated and 12 expressed arylsulfatases (RB4815, RB1477, RB5146, RB7875, RB13148, RB2357, RB348, RB3849, RB9091, RB9755, RB5355, RB3177, RB5294) (Table 3). RB9091 was only active in the case of chondroitin sulfate and λ-carrageenan and is so far functionally unknown from previous studies. Eight sulfatases have been exclusively expressed in chondroitin sulfate grown cells considering all tested substrates.