Structural Basis for Translation Termination on the 70S Ribosome

Journal Article · Wed May 20 04:00:00 EDT 2009 · Nature 454:852,2008

OSTI ID:953077

Laurberg, M; Asahara, H; Korostelev, A; Zhu, J; Trakhanov, S; Noller, H F

At termination of protein synthesis, type I release factors promote hydrolysis of the peptidyl-transfer RNA linkage in response to recognition of a stop codon. Here we describe the crystal structure of the Thermus thermophilus 70S ribosome in complex with the release factor RF1, tRNA and a messenger RNA containing a UAA stop codon, at 3.2 {angstrom} resolution. The stop codon is recognized in a pocket formed by conserved elements of RF1, including its PxT recognition motif, and 16S ribosomal RNA. The codon and the 30S subunit A site undergo an induced fit that results in stabilization of a conformation of RF1 that promotes its interaction with the peptidyl transferase centre. Unexpectedly, the main-chain amide group of Gln 230 in the universally conserved GGQ motif of the factor is positioned to contribute directly to peptidyl-tRNA hydrolysis.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 953077
• Report Number(s): SLAC-REPRINT-2009-207
• Journal Information: Nature 454:852,2008, Journal Name: Nature 454:852,2008 Vol. 454
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
AMIDES
CODONS
CRYSTAL STRUCTURE
HYDROLYSIS
MESSENGER-RNA
Other
OTHER
PROTEINS
RESOLUTION
RIBOSOMAL RNA
RIBOSOMES
RNA
STABILIZATION
SYNTHESIS
TRANSFERASES