title: X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit.
abstract: 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.
authors.affiliation: Max-Planck-Institute for Molecular Genetics, Berlin, Germany.
authors.forename: Daniel N
authors.initials: DN
authors.lastname: Wilson
authors.forename: Frank
authors.initials: F
authors.lastname: Schluenzen
authors.forename: Joerg M
authors.initials: JM
authors.lastname: Harms
authors.forename: Takuya
authors.initials: T
authors.lastname: Yoshida
authors.forename: Tadayasu
authors.initials: T
authors.lastname: Ohkubo
authors.forename: Renate
authors.initials: R
authors.lastname: Albrecht
authors.forename: Joerg
authors.initials: J
authors.lastname: Buerger
authors.forename: Yuji
authors.initials: Y
authors.lastname: Kobayashi
authors.forename: Paola
authors.initials: P
authors.lastname: Fucini
mesh_terms: 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
chemical_list: D011506:Proteins; D012269:Ribosomal Proteins; C087267:ribosome releasing factor