RRC ID 21538
著者 Kobayashi K, Saito K, Ishitani R, Ito K, Nureki O.
タイトル Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.
ジャーナル Nucleic Acids Res
Abstract When a stop codon appears at the ribosomal A site, the class I and II release factors (RFs) terminate translation. In eukaryotes and archaea, the class I and II RFs form a heterodimeric complex, and complete the overall translation termination process in a GTP-dependent manner. However, the structural mechanism of the translation termination by the class I and II RF complex remains unresolved. In archaea, archaeal elongation factor 1 alpha (aEF1α), a carrier GTPase for tRNA, acts as a class II RF by forming a heterodimeric complex with archaeal RF1 (aRF1). We report the crystal structure of the aRF1·aEF1α complex, the first active class I and II RF complex. This structure remarkably resembles the tRNA·EF-Tu complex, suggesting that aRF1 is efficiently delivered to the ribosomal A site, by mimicking tRNA. It provides insights into the mechanism that couples GTP hydrolysis by the class II RF to stop codon recognition and peptidyl-tRNA hydrolysis by the class I RF. We discuss the different mechanisms by which aEF1α recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1α.
巻・号 40(18)
ページ 9319-28
公開日 2012-10-1
DOI 10.1093/nar/gks660
PII gks660
PMID 22772989
PMC PMC3467058
MeSH Archaeal Proteins / chemistry* Archaeal Proteins / metabolism Codon, Terminator Guanosine Triphosphate / chemistry* Guanosine Triphosphate / metabolism Models, Molecular Peptide Chain Termination, Translational* Peptide Elongation Factor 1 / chemistry* Peptide Elongation Factor 1 / metabolism Peptide Elongation Factor Tu / chemistry Peptide Termination Factors / chemistry* Peptide Termination Factors / metabolism RNA, Transfer / chemistry Structural Homology, Protein
IF 11.502
引用数 22
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
遺伝子材料 Genomic DNA of Aeropyrum pernix JCM 9820T (JGD07499)
一般微生物