title: EF-G and EF4: translocation and back-translocation on the bacterial ribosome.
abstract: Ribosomes translate the codon sequence of an mRNA into the amino acid sequence of the corresponding protein. One of the most crucial events is the translocation reaction, which involves movement of both the mRNA and the attached tRNAs by one codon length and is catalysed by the GTPase elongation factor G (EF-G). Interestingly, recent studies have identified a structurally related GTPase, EF4, that catalyses movement of the tRNA2-mRNA complex in the opposite direction when the ribosome stalls, which is known as back-translocation. In this Review, we describe recent insights into the mechanistic basis of both translocation and back-translocation.
authors.affiliation: 1] Institut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. [2].
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Yamamoto
authors.affiliation: 1] Laboratory of noncoding RNA, Institute of Biophysics, Chinese Academy of Science; 15 Datun Road, Beijing 100101, China. [2].
authors.forename: Yan
authors.initials: Y
authors.lastname: Qin
authors.affiliation: 1] NOXXON Pharma AG, Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany. [2].
authors.forename: John
authors.initials: J
authors.lastname: Achenbach
authors.affiliation: Laboratory of noncoding RNA, Institute of Biophysics, Chinese Academy of Science; 15 Datun Road, Beijing 100101, China.
authors.forename: Chengmin
authors.initials: C
authors.lastname: Li
authors.affiliation: Max Planck Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany.
authors.forename: Jaroslaw
authors.initials: J
authors.lastname: Kijek
authors.affiliation: Institut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
authors.forename: Christian M T
authors.initials: CM
authors.lastname: Spahn
authors.affiliation: 1] Institut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. [2] Max Planck Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany.
authors.forename: Knud H
authors.initials: KH
authors.lastname: Nierhaus
mesh_terms: D001419:Bacteria / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D018988:Bacterial Translocation; D001665:Binding Sites; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D020653:Peptide Elongation Factor G / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D020653:Peptide Elongation Factor G; D012333:RNA, Messenger; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D020558:GTP Phosphohydrolases