Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (172K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (20)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by O’Connor, M.
Right arrow Articles by Dahlberg, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O’Connor, M.
Right arrow Articles by Dahlberg, A. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 3 710-715
© 2001 Oxford University Press

Mutagenesis of the peptidyltransferase center of 23S rRNA: the invariant U2449 is dispensable

Michael O’Connor*, Wyan-Ching Mimi Lee, Anuj Mankad, Catherine L. Squires1 and Albert E. Dahlberg

J. W. Wilson Laboratory, Department of Molecular and Cellular Biology and Biochemistry, Brown University, Providence, RI 02912, USA and 1Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA

U2449 is one of many invariant residues in the central loop of domain V of 23S rRNA, a region that constitutes part of the peptidyltransferase center of the ribosome. In Escherichia coli, this U is post-transcriptionally modified to dihydrouridine (D) and is the only D modification found in E.coli rRNAs. To analyze the role of this base and its modification in ribosomal function, all three base substitutions were constructed on a plasmid copy of the rrnB operon and assayed for their ability to support cell growth in a strain of E.coli lacking chromosomal rrn operons. Both purine substitution mutations were not viable. However, growth and antibiotic sensitivity of cells expressing only the mutant D2449C rRNA was indistinguishable from wild type. We conclude that while a pyrimidine is required at position 2449 for proper ribosomal function, the D modification is dispensable.

* To whom correspondence should be addressed. Tel: +1 401 863 3652; Fax: +1 401 863 1182; Email: michael_o'connor{at}brown.edu


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
N. S. Sato, N. Hirabayashi, I. Agmon, A. Yonath, and T. Suzuki
Comprehensive genetic selection revealed essential bases in the peptidyl-transferase center
PNAS, October 17, 2006; 103(42): 15386 - 15391.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. A. Bayfield, J. Thompson, and A. E. Dahlberg
The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation
Nucleic Acids Res., October 12, 2004; 32(18): 5512 - 5518.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
G. W. Novotny, L. Jakobsen, N. M. Andersen, J. Poehlsgaard, and S. Douthwaite
Ketolide Antimicrobial Activity Persists after Disruption of Interactions with Domain II of 23S rRNA
Antimicrob. Agents Chemother., October 1, 2004; 48(10): 3677 - 3683.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. E. Hesslein, V. I. Katunin, M. Beringer, A. B. Kosek, M. V. Rodnina, and S. A. Strobel
Exploration of the conserved A+C wobble pair within the ribosomal peptidyl transferase center using affinity purified mutant ribosomes
Nucleic Acids Res., July 15, 2004; 32(12): 3760 - 3770.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Dresios, P. Panopoulos, K. Suzuki, and D. Synetos
A Dispensable Yeast Ribosomal Protein Optimizes Peptidyltransferase Activity and Affects Translocation
J. Biol. Chem., January 24, 2003; 278(5): 3314 - 3322.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
K. Lee, C. A. Holland-Staley, and P. R. Cunningham
Genetic Approaches to Studying Protein Synthesis: Effects of Mutations at {Psi}516 and A535 in Escherichia coli 16S rRNA
J. Nutr., November 1, 2001; 131(11): 2994S - 3004.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Thompson, D. F. Kim, M. O'Connor, K. R. Lieberman, M. A. Bayfield, S. T. Gregory, R. Green, H. F. Noller, and A. E. Dahlberg
Analysis of mutations at residues A2451 and G2447 of 23S rRNA in the peptidyltransferase active site of the 50S ribosomal subunit
PNAS, July 19, 2001; (2001) 151257098.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. O'Connor and A. E. Dahlberg
Enhancement of translation by the epsilon element is independent of the sequence of the 460 region of 16S rRNA
Nucleic Acids Res., April 1, 2001; 29(7): 1420 - 1425.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Thompson, D. F. Kim, M. O'Connor, K. R. Lieberman, M. A. Bayfield, S. T. Gregory, R. Green, H. F. Noller, and A. E. Dahlberg
Analysis of mutations at residues A2451 and G2447 of 23S rRNA in the peptidyltransferase active site of the 50S ribosomal subunit
PNAS, July 31, 2001; 98(16): 9002 - 9007.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.