TY - JOUR
T1 - Staphylococcus aureus domain V functions in Escherichia coli ribosomes provided a conserved interaction with domain IV is restored
AU - Thompson, Jill
AU - Tapprich, William E.
AU - Munger, Corey
AU - Dahlberg, Albert E.
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
KW - Hybrid ribosomes
KW - Large ribosomal subunit
KW - Pathogenic bacteria
KW - Peptidyl transferase center
KW - Ribosomal RNA
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U2 - 10.1017/S1355838201010172
DO - 10.1017/S1355838201010172
M3 - Article
C2 - 11497427
AN - SCOPUS:0034903227
SN - 1355-8382
VL - 7
SP - 1076
EP - 1083
JO - RNA
JF - RNA
IS - 8
ER -