Staphylococcus aureus domain V functions in Escherichia coli ribosomes provided a conserved interaction with domain IV is restored.
Domain V of Escherichia coli 23 S rRNA (residues 2023-2630) was replaced by that from Staphylococcus aureus, thereby introducing 132 changes in the rRNA sequence. The resulting ribosomal mutant was unable to support cell growth. The mutant was rescued, however, by restoring an interaction between domains IV and V (residues 1782 and 2586). Although the importance of this interaction, U/U in E. coli, C/C in S. aureus, is therefore demonstrated, it cannot be the only tertiary interaction important for ribosomal function as the rescued hybrid grew more slowly than the wild type. Additionally, although the single-site mutations U1782C and U2586C in E. coli are viable, the double mutant is lethal.
Thompson
J
J
Department of Molecular and Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA. Jill_Rosemary_Thompson@brown.edu
Tapprich
W E
WE
Munger
C
C
Dahlberg
A E
AE
D001483:Base Sequence; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009690:Nucleic Acid Conformation; D010957:Plasmids / Q000378:metabolism; D017354:Point Mutation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D012335:RNA, Ribosomal / Q000378:metabolism; D012338:RNA, Ribosomal, 23S / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000378:metabolism
D012335:RNA, Ribosomal; D012338:RNA, Ribosomal, 23S; D012313:RNA