X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit.
This study presents the crystal structure of domain I of the Escherichia coli ribosome recycling factor (RRF) bound to the Deinococcus radiodurans 50S subunit. The orientation of RRF is consistent with the position determined on a 70S-RRF complex by cryoelectron microscopy (cryo-EM). Alignment, however, requires a rotation of 7 degrees and a shift of the cryo-EM RRF by a complete turn of an alpha-helix, redefining the contacts established with ribosomal components. At 3.3 A resolution, RRF is seen to interact exclusively with ribosomal elements associated with tRNA binding and/or translocation. Furthermore, these results now provide a high-resolution structural description of the conformational changes that were suspected to occur on the 70S-RRF complex, which has implications for the synergistic action of RRF with elongation factor G (EF-G). Specifically, the tip of the universal bridge element H69 is shifted by 20 A toward h44 of the 30S subunit, suggesting that RRF primes the intersubunit bridge B2a for the action of EF-G. Collectively, our data enable a model to be proposed for the dual action of EF-G and RRF during ribosome recycling.
Wilson
Daniel N
DN
Max-Planck-Institute for Molecular Genetics, Berlin, Germany.
Schluenzen
Frank
F
Harms
Joerg M
JM
Yoshida
Takuya
T
Ohkubo
Tadayasu
T
Albrecht
Renate
R
Buerger
Joerg
J
Kobayashi
Yuji
Y
Fucini
Paola
P
D000595:Amino Acid Sequence; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D012269:Ribosomal Proteins; D012270:Ribosomes / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D011506:Proteins; D012269:Ribosomal Proteins; C087267:ribosome releasing factor