title: RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors.
abstract: During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a GTP-dependent manner. We present the crystal structure of E. coli RF3*GDP, which has a three-domain architecture strikingly similar to the structure of EF-Tu*GTP. Biochemical data on RF3 mutants show that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3. Furthermore, we present a cryo-electron microscopy (cryo-EM) structure of the posttermination ribosome bound with RF3 in the GTP form. Our data show that RF3*GTP binding induces large conformational changes in the ribosome, which break the interactions of the class I RF with both the decoding center and the GTPase-associated center of the ribosome, apparently leading to the release of the class I RF.
authors.affiliation: Howard Hughes Medical Institute, Health Research, Inc. at the Wadsworth Center, Empire State Plaza, Albany, NY 12201-0509, USA.
authors.forename: Haixiao
authors.initials: H
authors.lastname: Gao
authors.forename: Zhihong
authors.initials: Z
authors.lastname: Zhou
authors.forename: Urmila
authors.initials: U
authors.lastname: Rawat
authors.forename: Chenhui
authors.initials: C
authors.lastname: Huang
authors.forename: Lamine
authors.initials: L
authors.lastname: Bouakaz
authors.forename: Chernhoe
authors.initials: C
authors.lastname: Wang
authors.forename: Zhihong
authors.initials: Z
authors.lastname: Cheng
authors.forename: Yuying
authors.initials: Y
authors.lastname: Liu
authors.forename: Andrey
authors.initials: A
authors.lastname: Zavialov
authors.forename: Richard
authors.initials: R
authors.lastname: Gursky
authors.forename: Suparna
authors.initials: S
authors.lastname: Sanyal
authors.forename: Måns
authors.initials: M
authors.lastname: Ehrenberg
authors.forename: Joachim
authors.initials: J
authors.lastname: Frank
authors.forename: Haiwei
authors.initials: H
authors.lastname: Song
mesh_terms: D001665:Binding Sites; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D009154:Mutation; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D010454:Peptide Termination Factors; C489007:prfC protein, E coli; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu