Mutations in the GTPase center of Escherichia coli 23S rRNA indicate release factor 2-interactive sites.
Mutations in the GTPase center of Escherichia coli 23S rRNA were characterized in vivo as UGA-specific nonsense suppressors. Some site-directed mutations did not exhibit suppressor activity and were interspersed among suppressor mutations. Our results demonstrate the involvement of the two adjacent loops of this conserved rRNA structure in UGA-dependent translation termination and, taken with previous in vitro analyses and with consideration of the crystal structure of the GTPase center RNA, indicate that nucleotides 1067, 1093, 1094, and 1095 are sites of interaction with release factor 2.
Xu
Wenbing
W
Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
Pagel
Frances T
FT
Murgola
Emanuel J
EJ
D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics* / Q000254:growth & development; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D010454:Peptide Termination Factors / Q000378:metabolism*; D012329:RNA, Bacterial / Q000737:chemistry; D012338:RNA, Ribosomal, 23S / Q000737:chemistry; D012269:Ribosomal Proteins / Q000378:metabolism*; D012407:rRNA Operon
D010454:Peptide Termination Factors; D012329:RNA, Bacterial; D012338:RNA, Ribosomal, 23S; D012269:Ribosomal Proteins; C041460:peptide chain termination release factor 2; D020558:GTP Phosphohydrolases