PubMedCrossRef 39. Gmür R, Guggenheim B: Antigenic heterogeneity of Bacteroides intermedius as recognized by monoclonal antibodies. Infect Immun 1983, 42:459–470.PubMed 40. Thurnheer T, Guggenheim B, Gruica B, Gmür R: Infinite

serovar and ribotype heterogeneity among oral Fusobacterium nucleatum strains? Anaerobe 1999, 5:79–92.CrossRef 41. Thurnheer T, Guggenheim B, Gmür R: Characterization of monoclonal antibodies for rapid identification of Actinomyces naeslundii in clinical samples. FEMS Microbiol Lett 1997, 150:255–262.PubMedCrossRef Authors’ contributions TWA designed the study, executed the experiments and drafted MK-0518 solubility dmso the manuscript. TT and RG supervised the study and edited the manuscript draft. All authors read and approved the final manuscript.”
“Background The fidelity of the translation process depends on the aminoacyl–tRNA synthetase enzymes (aaRS). These essential enzymes are responsible for the correct attachment of the selleck kinase inhibitor corresponding amino acid onto the cognate tRNA, therefore organisms have at least 20 synthetases [1]. The enzymes are divided in two classes, each class having a conserved structure. The genes encoding the aaRS are easily detected within sequenced genomes [2, 3], and some species contain synthetase gene duplications, such as the glutamyl-tRNA synthetases (GluRS) in Acidithiobacillus ferrooxidans and Helicobacter pylori (genes gltX1 and gltX2) [4,

5]. aaRS paralogs, predicted sequences with homology to Thiazovivin fragments of synthetases, have also been identified, which is not surprising given the modular nature of the aaRS [6]. Some of the paralogs may be pseudogenes while others have known functions. For instance HisZ from Lactococcus lactis, which has similarity with the catalytic domain of histidyl-tRNA synthetase, is involved in histidine biosynthesis [7]. A recent study in Salmonella enterica has shown that PoxA, encoded by poxA/genX, has similarity to the carboxy-terminal Rutecarpine catalytic domain of lysine-tRNA synthetase and is required for posttranslational aminoacylation of bacterial

elongation factor P. A poxA mutant has reduced colonization and virulence, possibly due to misregulated expression of proteins encoded by the SPI-1 pathogenicity island [8, 9]. An Escherichia coli glutamyl-tRNA synthetase paralog, glutamyl queuosine-tRNAAsp synthetase (GluQ-RS) has approximately 35% amino acid similarity with the catalytic domain of GluRS. This includes the amino acids involved in recognition and activation of glutamate. Although GluQ-RS is missing the carboxyl-terminus domain responsible for the tRNA recognition, in E. coli this enzyme is able to activate the amino acid in the absence of the tRNA. Further, once the aminoacyl-adenylate has been formed, the enzyme attaches the glutamate to the nucleoside queuosine present onto the tRNAAsp. Therefore, this enzyme is involved in the synthesis of a new modified nucleoside glutamyl-queuosine (GluQ) present in tRNAAsp[10, 11].