Crystal structure of the ribosome recycling factor bound to the ribosome.
In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNA(fMet) in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Albert
A
Weixlbaumer
Sabine
S
Petry
Christine M
CM
Dunham
Maria
M
Selmer
Ann C
AC
Kelley
V
V
Ramakrishnan
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012329:RNA, Bacterial / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry*; D016963:Thermus thermophilus
D008024:Ligands; D012329:RNA, Bacterial; D012269:Ribosomal Proteins; C087267:ribosome releasing factor