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Staphylococcus aureus domain V functions in Escherichia coli ribosomes provided a conserved interaction with domain IV is restored

Published online by Cambridge University Press:  27 July 2001

JILL THOMPSON ,
WILLIAM E. TAPPRICH ,
COREY MUNGER  and
ALBERT E. DAHLBERG
JILL THOMPSON
Affiliation:
Department of Molecular and Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA
WILLIAM E. TAPPRICH
Affiliation:
Department of Biology, University of Nebraska at Omaha, Omaha, Nebraska 68182, USA
COREY MUNGER
Affiliation:
Department of Biology, University of Nebraska at Omaha, Omaha, Nebraska 68182, USA
ALBERT E. DAHLBERG
Affiliation:
Department of Molecular and Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA
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Abstract

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.

Keywords

hybrid ribosomeslarge ribosomal subunitpathogenic bacteriapeptidyl transferase centerribosomal RNA
Type
REPORTS
Information
RNA , Volume 7 , Issue 8 , August 2001 , pp. 1076 - 1083
Copyright
© 2001 RNA Society

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