The results obtained suggest that the mannosylated fusion protein improve the immunogenicity of the conjugated OVA

ase system, they do not have an ubiquitin-dependent protein degradation system like in eukaryotes. Still several bacteria have in their genome typical eukaryotic E3 ubiquitin ligase-like proteins among which F-box proteins, like the GALA proteins from R. solanacearum. These bacterial F-box proteins also often contain eukaryote-like protein-protein interaction BS-181 chemical information domains like LRR, ankyrin and WD40. We systematically searched all the sequenced eubacterial genomes available for the presence of the F-box domain service available at TIGR CMR). 23863710 We only found F-box domains present in one chlamydiae species out of 11 complete sequence available and in 9 proteobacteria out of 184 complete sequences available. All these positive hits correspond indeed to the presence of a canonical F-box domain. The evidence for functional F-box domains is available for both A. tumefaciens and R. solanacearum F-box containing proteins. A few low scoring hits were inspected and clearly ruled out as being F-box domains. Within the proteobacteria phylum, 9 out of 184 completely sequenced bacteria clearly contain at least one F-box-containing predicted protein. Among the 175 negatively scoring bacteria, we believe we can rule out the presence of ��remnants��of F-box domain, which could have been indicative of gene loss. Considering such sporadic presence of this F-box domain, the scenario of systematic gene loss appears very unlikely The F-box domain has its only described function in eukaryotic cells and is overrepresented in this kingdom hits: 735 in A. thaliana, 428 in Caenorhabditis elegans, 120 in humans, and only 46 hits among all bacteria sequence available, mostly in proteobacteria, see above). It is interesting to mention that all the bacteria containing F-box domains in their genome intimately interact with eukaryotes. For example, P. amoebophila, S. glossinidius and M. loti are symbionts of amoeba, insects and plants; A. tumefaciens, R. Solanacearum, P. syringae, X. campestris and X. axonopodis are plant pathogens and C. burnetii and L. pneumophila are human pathogens. Finally, for several of these F-box-containing bacterial proteins injection into their host cells has been proven or predicted . Among the seven GALA genes from 1828342 the R. solanacearum genome, GALA1 is located in an alternative codon usage region, GALA2 is flanked by a region duplicated elsewhere in the genome and GALA3 is flanked at either side by an alternative codon usage region. These genomic characteristic have been previously identified as potential signatures of LGT. Furthermore, considering the capacity of R. solanacearum to uptake DNA, it is natural to suggest a lateral gene transfer from host plant DNA that gave rise to the F-box domain of the GALA proteins. One way of testing such a hypothesis is through phylogenetic analysis of the protein origins to identify putative donor for a Evolution of GALA Proteins conclusion is supported by the fact that two plant F-box-LRR proteins have a couple of GALA-LRRs inserted in GL-LRR tandem arrays. Considering that CC-LRRs are much more abundant in plants than GALA-LRRs, and based on the above-mentioned facts, we propose the following sequence of evolutionary events that could ��transform��the CC-LRR into GALA-LRR tandem arrays. First, the accumulation of point mutations may lead to the spontaneous occurrence of the first GALA-LRR and due to the structural complementarities between this new LRR and the CC-LRRs the occurrence of GALA-LRR does not signific

Leave a Reply