Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (80K) 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 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 (28)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kowalak, J.
Right arrow Articles by McCloskey, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kowalak, J.
Right arrow Articles by McCloskey, J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 24, Issue 4 688-693, Copyright © 1996 by Oxford University Press


ARTICLES

Structural characterization of U*-1915 in domain IV from Escherichia coli 23S ribosomal RNA as 3-methylpseudouridine

JA Kowalak, E Bruenger, T Hashizume, JM Peltier, J Ofengand and JA McCloskey
Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.

Mass spectrometry-based methods have been used to study post- transcriptional modification in the 1900-1974 nt segment of domain IV in 23S rRNA of Escherichia coli, a region which interacts with domain V in forming the three- dimensional structure of the peptidyl transferase center within the ribosome. A nucleoside constituent of M r 258 (U*)which occurs at position 1915, within the highly modified oligonucleotide sequence 1911-psiAACU*Apsi-1917, was characterized as 3- methylpseudouridine (m3psi). The assignment was confirmed by chemical synthesis of m3psi and comparison with the natural nucleoside by liquid chromatography-mass spectrometry. 3-Methylpseudouridine is previously unknown in nature and is the only known derivative of the common modified nucleoside pseudouridine thus far found in bacterial rRNA.
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
RNAHome page
R. Ero, L. Peil, A. Liiv, and J. Remme
Identification of pseudouridine methyltransferase in Escherichia coli
RNA, October 1, 2008; 14(10): 2223 - 2233.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
E. Purta, K. H. Kaminska, J. M. Kasprzak, J. M. Bujnicki, and S. Douthwaite
YbeA is the m3{Psi} methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA
RNA, October 1, 2008; 14(10): 2234 - 2244.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
S. C. Abeysirigunawardena and C. S. Chow
pH-dependent structural changes of helix 69 from Escherichia coli 23S ribosomal RNA
RNA, April 1, 2008; 14(4): 782 - 792.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
M. SUMITA, J.-P. DESAULNIERS, Y.-C. CHANG, H. M.-P. CHUI, L. CLOS II, and C. S. CHOW
Effects of nucleotide substitution and modification on the stability and structure of helix 69 from 28S rRNA
RNA, September 1, 2005; 11(9): 1420 - 1429.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
M. DEL CAMPO, C. RECINOS, G. YANEZ, S. C. POMERANTZ, R. GUYMON, P. F. CRAIN, J. A. MCCLOSKEY, and J. OFENGAND
Number, position, and significance of the pseudouridines in the large subunit ribosomal RNA of Haloarcula marismortui and Deinococcus radiodurans
RNA, February 1, 2005; 11(2): 210 - 219.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
M. DEL CAMPO, J. OFENGAND, and A. MALHOTRA
Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli
RNA, February 1, 2004; 10(2): 231 - 239.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
K. G. Patteson, L. P. Rodicio, and P. A. Limbach
Identification of the mass-silent post-transcriptionally modified nucleoside pseudouridine in RNA by matrix-assisted laser desorption/ionization mass spectrometry
Nucleic Acids Res., May 15, 2001; 29(10): e49 - e49.
[Abstract] [Full Text] [PDF]


Home page
Cold Spring Harb Symp Quant BiolHome page
J. OFENGAND, A. MALHOTRA, J. REMME, N.S. GUTGSELL, M. DEL CAMPO, S. JEAN-CHARLES, L. PEIL, and Y. KAYA
Pseudouridines and Pseudouridine Synthases of the Ribosome
Cold Spring Harb Symp Quant Biol, January 1, 2001; 66(0): 147 - 160.
[Abstract] [PDF]


Home page
Nucleic Acids ResHome page
M. Meroueh, P. J. Grohar, J. Qiu, J. SantaLucia Jr, S. A. Scaringe, and C. S. Chow
Unique structural and stabilizing roles for the individual pseudouridine residues in the 1920 region of Escherichia coli 23S rRNA
Nucleic Acids Res., May 15, 2000; 28(10): 2075 - 2083.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
Y. Zebarjadian, T. King, M. J. Fournier, L. Clarke, and J. Carbon
Point Mutations in Yeast CBF5 Can Abolish In Vivo Pseudouridylation of rRNA
Mol. Cell. Biol., November 1, 1999; 19(11): 7461 - 7472.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Conrad, D. Sun, N. Englund, and J. Ofengand
The rluC Gene of Escherichia coli Codes for a Pseudouridine Synthase That Is Solely Responsible for Synthesis of Pseudouridine at Positions 955, 2504, and 2580 in 23 S Ribosomal RNA
J. Biol. Chem., July 17, 1998; 273(29): 18562 - 18566.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. A. Kowalak, E. Bruenger, P. F. Crain, and J. A. McCloskey
Identities and Phylogenetic Comparisons of Posttranscriptional Modifications in 16 S Ribosomal RNA from Haloferax volcanii
J. Biol. Chem., August 4, 2000; 275(32): 24484 - 24489.
[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.