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References (12)
-
H Kamiya, E Iida, N Murata-Kamiya, Y Yamamoto, T Miki, H Harashima (2003)
Suppression of spontaneous and hydrogen peroxide-induced mutations by a MutT-type nucleotide pool sanitization enzyme, the Escherichia coli Orf135 proteinGenes Cells, 8
-
TD Goddard, DG Kneller (1999)
SPARKY3 -
AS Mildvan, Z Xia, HF Azurmendi, V Saraswat, PM Legler, MA Massiah, SB Gabelli, MA Bianchet, LW Kang, LM Amzel (2005)
Structures and mechanisms of Nudix hydrolasesArch Biochem Biophys, 433
-
F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer, A Bax (1995)
NMRPipe: a multidimensional spectral processing system based on UNIX pipesJ Biomol NMR, 6
-
H Kamiya, E Iida, H Harashima (2004)
Important amino acids in the phosphohydrolase module of Escherichia coli Orf135Biochem Biophys Res Commun, 323
-
G Cornilescu, F Delaglio, A Bax (1999)
Protein backbone angle restraints from searching a database for chemical shift and sequence homologyJ Biomol NMR, 13
-
JL Markley, A Bax, Y Arata, CW Hilbers, R Kaptein, BD Sykes, PE Wright, K Wuthrich (1998)
Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopyJ Biomol NMR, 12
-
E Iida, K Satou, M Mishima, C Kojima, H Harashima, H Kamiya (2005)
Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 proteinBiochemistry, 44
-
H Kamiya, N Murata-Kamiya, E Iida, H Harashima (2001)
Hydrolysis of oxidized nucleotides by the Escherichia coli Orf135 proteinBiochem Biophys Res Commun, 288
-
SF O’Handley, CA Dunn, MJ Bessman (2001)
Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTPJ Biol Chem, 276
-
K Fujikawa, H Kasai (2002)
The oxidized pyrimidine ribonucleotide, 5-hydroxy-CTP, is hydrolyzed efficiently by the Escherichia coli recombinant Orf135 proteinDNA Repair (Amst), 1
-
M Sattler, J Schleucher, C Griesinger (1999)
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradientsProg Nucl Magn Reson Spectrosc, 34
- Publisher
- Springer Journals
- Copyright
- Copyright © 2011 by Springer Science+Business Media B.V.
- Subject
- Physics; Polymer Sciences; Biochemistry, general; Biophysics and Biological Physics
- ISSN
- 1874-2718
- eISSN
- 1874-270X
- DOI
- 10.1007/s12104-011-9312-7
- pmid
- 21553121
- Publisher site
- See Article on Publisher Site
Abstract
Escherichia coli Orf135 protein is thought to be an enzyme that efficiently hydrolyzes oxidatively damaged nucleotides such as 2-hydroxy-dATP, 8-hydroxy-dGTP and 5-hydroxy-CTP, in addition to 5-methyl-dCTP, dCTP and CTP, thus preventing mutations in cells caused by unfavorable base pairing. Nucleotide pool sanitization by Orf135 is important since organisms are continually subjected to potential damage by reactive oxygen species produced during respiration. It is known that the frequency of spontaneous and H2O2-induced mutations is two to threefold higher in the orf135 - strain compared with the wild-type. Orf135 is a member of the Nudix family of proteins which hydrolyze nucleoside diphosphate derivatives. Nudix hydrolases are characterized by the presence of a conserved motif, although they recognize various substrates and possess a variety of substrate binding pockets. We are interested in delineating the mechanism by which Orf135 recognizes oxidatively damaged nucleotides. To this end, we are investigating the tertiary structure of Orf135 and its interaction with substrate using NMR. Herein, we report on the 1H, 13C and 15N resonance assignments of Orf135, which should contribute towards a structural understanding of Orf135 and its interaction with substrate.
Journal
Biomolecular NMR Assignments – Springer Journals
Published: May 7, 2011