1: J Bacteriol. 2006 Dec 15; [Epub ahead of print] Loss of a universal tRNA feature. Wang C, Sobral BW, Williams KP. Virginia Bioinformatics Institute, Virginia Polytechnic Institute and State University, Blacksburg VA 24061. tRNA(His) has always hitherto been found with one of the most distinctive of tRNA features, an extra 5 nucleotide that is usually a guanylate. tRNA(His) genes in a disjoint alphaproteobacterial group comprising the Rhizobiales, Rhodobacterales, Caulobacterales, Parvularculales and Pelagibacter generally fail to encode this extra guanylate, unlike those of other alphaproteobacteria and bacteria in general. Rather than adding an extra 5 guanylate posttranscriptionally as eukaryotes do, evidence is presented that two of these species, Sinorhizobium meliloti and Caulobacter crescentus, simply lack any extra nucleotide on tRNA(His). This loss correlates with changes at the 3 end sequence of tRNA(His) and at many sites in histidyl-tRNA synthetase that might be expected to affect tRNA(His) recognition, in the flipping loop, the insertion domain, the anticodon-binding domain, and in the motif 2 loop. The altered tRNA charging system may have affected other tRNA charging systems in these bacteria; for example, a site in tRNA(Glu) sequences was found to covary with tRNA(His) among alphaproteobacteria. PMID: 17172343 [PubMed - as supplied by publisher] Related Links Protein signatures distinctive of alpha proteobacteria and its subgroups and a model for alpha-proteobacterial evolution. [Crit Rev Microbiol. 2005] PMID:15986834 TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase. [Nucleic Acids Res. 2006] PMID:16473847 tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. [RNA. 2006] PMID:16625026 Function of the extra 5'-phosphate carried by histidine tRNA. [Biochemistry. 2000] PMID:10747795 The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity. [Biochemistry. 2006] PMID:16800632