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Title: Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA

Abstract

Pseudouridine synthases catalyze the isomerization of uridine to pseudouridine ({psi}) in rRNA and tRNA. The pseudouridine synthase RluF from Escherichia coli (E.C. 4.2.1.70) modifies U2604 in 23S rRNA, and belongs to a large family of pseudouridine synthases present in all kingdoms of life. Here we report the domain architecture and crystal structure of the catalytic domain of E. coli RluF at 2.6 Angstroms resolution. Limited proteolysis, mass spectrometry and N-terminal sequencing indicate that RluF has a distinct domain architecture, with the catalytic domain flanked at the N and C termini by additional domains connected to it by flexible linkers. The structure of the catalytic domain of RluF is similar to those of RsuA and TruB. RluF is a member of the RsuA sequence family of {psi}-synthases, along with RluB and RluE. Structural comparison of RluF with its closest structural homologues, RsuA and TruB, suggests possible functional roles for the N-terminal and C-terminal domains of RluF.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914154
Report Number(s):
BNL-78722-2007-JA
Journal ID: ISSN 0022-2836; JMOBAK; TRN: US0801580
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
J. Mol. Biol.
Additional Journal Information:
Journal Volume: 359; Journal Issue: 4; Journal ID: ISSN 0022-2836
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 43 PARTICLE ACCELERATORS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; FUNCTIONALS; ISOMERIZATION; MASS SPECTROSCOPY; PROTEOLYSIS; RESOLUTION; URIDINE; NSLS; national synchrotron light source

Citation Formats

Sunita, S, Zhenxing, H, Swaathi, J, Cygler, M, Matte, A, and Sivaraman, J. Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA. United States: N. p., 2006. Web. doi:10.1016/j.jmb.2006.04.019.
Sunita, S, Zhenxing, H, Swaathi, J, Cygler, M, Matte, A, & Sivaraman, J. Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA. United States. https://doi.org/10.1016/j.jmb.2006.04.019
Sunita, S, Zhenxing, H, Swaathi, J, Cygler, M, Matte, A, and Sivaraman, J. 2006. "Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA". United States. https://doi.org/10.1016/j.jmb.2006.04.019.
@article{osti_914154,
title = {Domain organization and crystal structure of the catalytic domain of E.coli RluF, a pseudouridine synthase that acts on 23S rRNA},
author = {Sunita, S and Zhenxing, H and Swaathi, J and Cygler, M and Matte, A and Sivaraman, J},
abstractNote = {Pseudouridine synthases catalyze the isomerization of uridine to pseudouridine ({psi}) in rRNA and tRNA. The pseudouridine synthase RluF from Escherichia coli (E.C. 4.2.1.70) modifies U2604 in 23S rRNA, and belongs to a large family of pseudouridine synthases present in all kingdoms of life. Here we report the domain architecture and crystal structure of the catalytic domain of E. coli RluF at 2.6 Angstroms resolution. Limited proteolysis, mass spectrometry and N-terminal sequencing indicate that RluF has a distinct domain architecture, with the catalytic domain flanked at the N and C termini by additional domains connected to it by flexible linkers. The structure of the catalytic domain of RluF is similar to those of RsuA and TruB. RluF is a member of the RsuA sequence family of {psi}-synthases, along with RluB and RluE. Structural comparison of RluF with its closest structural homologues, RsuA and TruB, suggests possible functional roles for the N-terminal and C-terminal domains of RluF.},
doi = {10.1016/j.jmb.2006.04.019},
url = {https://www.osti.gov/biblio/914154}, journal = {J. Mol. Biol.},
issn = {0022-2836},
number = 4,
volume = 359,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}