dc.creator | Korencic, D. | en |
dc.creator | Ahel, I. | en |
dc.creator | Schelert, J. | en |
dc.creator | Sacher, M. | en |
dc.creator | Ruan, B. | en |
dc.creator | Stathopoulos, C. | en |
dc.creator | Blum, P. | en |
dc.creator | Ibba, M. | en |
dc.creator | Söll, D. | en |
dc.date.accessioned | 2015-11-23T10:35:34Z | |
dc.date.available | 2015-11-23T10:35:34Z | |
dc.date.issued | 2004 | |
dc.identifier | 10.1073/pnas.0403926101 | |
dc.identifier.issn | 278424 | |
dc.identifier.uri | http://hdl.handle.net/11615/29633 | |
dc.description.abstract | Threonyl-tRNA synthetase (ThrRS) participates in protein synthesis quality control by selectively editing the misacylated species Ser-tRNAThr. In bacteria and eukaryotes the editing function of ThrRS resides in a highly conserved N-terminal domain distant from the active site. Most archaeal ThrRS proteins are devoid of this editing domain, suggesting evolutionary divergence of quality-control mechanisms. Here we show that archaeal editing of Ser-tRNAThr is catalyzed by a domain unrelated to, and absent from, bacterial and eukaryotic ThrRSs. Despite the lack of sequence homology, the archaeal and bacterial editing domains are both reliant on a pair of essential histidine residues suggestive of a common catalytic mechanism. Whereas the archaeal editing module is most commonly part of full-length ThrRS, several crenarchaeal species contain individual genes encoding the catalytic (ThrRS-cat) and editing domains (ThrRS-ed). Sulfolobus solfataricus ThrRS-cat was shown to synthesize both Thr-tRNAThr and Ser-tRNAThr and to lack editing activity against Ser-tRNAThr. In contrast, ThrRS-ed lacks aminoacylation activity but can act as an autonomous protein in trans to hydrolyze specifically Ser-tRNAThr, or it can be fused to ThrRS-cat to provide the same function in cis. Deletion analyses indicate that ThrRS-ed is dispensable for growth of S.solfataricus under standard conditions but is required for normal growth in media with elevated serine levels. The growth phenotype of the ThrRS-ed deletion strain suggests that retention of the discontinuous ThrRS quaternary structure relates to specific physiological requirements still evident in certain Archaea. | en |
dc.source | Proceedings of the National Academy of Sciences of the United States of America | en |
dc.source.uri | http://www.scopus.com/inward/record.url?eid=2-s2.0-3142704216&partnerID=40&md5=1dcd0642fc5c0be7b653e4e0217272e9 | |
dc.subject | threonine transfer RNA | en |
dc.subject | acylation | en |
dc.subject | Archaebacterium | en |
dc.subject | article | en |
dc.subject | bacterial growth | en |
dc.subject | catalysis | en |
dc.subject | eukaryote evolution | en |
dc.subject | gene deletion | en |
dc.subject | nonhuman | en |
dc.subject | nucleotide sequence | en |
dc.subject | priority journal | en |
dc.subject | protein domain | en |
dc.subject | protein quality | en |
dc.subject | protein synthesis regulation | en |
dc.subject | quality control | en |
dc.subject | RNA editing | en |
dc.subject | sequence homology | en |
dc.subject | site directed mutagenesis | en |
dc.subject | Sulfolobus solfataricus | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Chimera | en |
dc.subject | Gene Expression Regulation, Archaeal | en |
dc.subject | Hydrolysis | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | Protein Biosynthesis | en |
dc.subject | Protein Structure, Tertiary | en |
dc.subject | RNA, Transfer, Amino Acyl | en |
dc.subject | Sequence Homology, Amino Acid | en |
dc.subject | Serine | en |
dc.subject | Sulfolobus | en |
dc.subject | Threonine | en |
dc.subject | Threonine-tRNA Ligase | en |
dc.subject | Archaea | en |
dc.subject | Bacteria (microorganisms) | en |
dc.subject | Eukaryota | en |
dc.subject | Felis catus | en |
dc.title | A freestanding proofreading domain is required for protein synthesis quality control in Archaea | en |
dc.type | journalArticle | en |