title: The unusual methanogenic seryl-tRNA synthetase recognizes tRNASer species from all three kingdoms of life.
abstract: The methanogenic archaea Methanococcus jannaschii and M. maripaludis contain an atypical seryl-tRNA synthetase (SerRS), which recognizes eukaryotic and bacterial tRNAsSer, in addition to the homologous tRNASer and tRNASec species. The relative flexibility in tRNA recognition displayed by methanogenic SerRSs, shown by aminoacylation and gel mobility shift assays, indicates the conservation of some serine determinants in all three domains. The complex of M. maripaludis SerRS with the homologues tRNASer was isolated by gel filtration chromatography. Complex formation strongly depends on the conformation of tRNA. Therefore, the renaturation conditions for in vitro transcribed tRNASer(GCU) isoacceptor were studied carefully. This tRNA, unlike many other tRNAs, is prone to dimerization, possibly due to several stretches of complementary oligonucleotides within its sequence. Dimerization is facilitated by increased tRNA concentration and can be diminished by fast renaturation in the presence of 5 mm magnesium chloride.
authors.affiliation: Department of Chemistry, Faculty of Science, University of Zagreb, Croatia.
authors.forename: Silvija
authors.initials: S
authors.lastname: Bilokapic
authors.forename: Dragana
authors.initials: D
authors.lastname: Korencic
authors.forename: Dieter
authors.initials: D
authors.lastname: Söll
authors.forename: Ivana
authors.initials: I
authors.lastname: Weygand-Durasevic
mesh_terms: D000926:Anticodon / Q000235:genetics; D001483:Base Sequence; D002850:Chromatography, Gel; D019281:Dimerization; D024202:Electrophoretic Mobility Shift Assay; D004926:Escherichia coli / Q000201:enzymology; D007525:Isoelectric Focusing; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism; D012362:RNA, Transfer, Ser / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D012714:Serine-tRNA Ligase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D014158:Transcription, Genetic; D015003:Yeasts / Q000201:enzymology
chemical_list: D000926:Anticodon; D012346:RNA, Transfer, Amino Acyl; D012362:RNA, Transfer, Ser; D012694:Serine; D012714:Serine-tRNA Ligase