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Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
Open accessAbstract
The Escherichia coli peptide methionine sulfoxide reductase gene (msrA) encodes a single-subunit polypeptide of 212 amino acid residues (M. A. Rahman, H. Nelson, H. Weissbach, and N. Brot, J. Biol. Chem. 267:15549-15551, 1992). RNA blot analysis showed that the gene is transcribed into an mRNA of about 850 nucleotides. The promoter region was characterized, and the transcription initiation site was identified by primer extension. The synthesis of the MsrA protein increased about threefold in a growth-phase-dependent fashion. In an attempt to define the in vivo role of msrA, a chromosomal disruption was constructed. This mutant was more sensitive to oxidative stress, suggesting that oxidation of methionine in proteins plays an important role in oxidative damage.
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“Significantly, methionine sulfoxide reductase knockout bacteria are sensitized to the cell killing effects of hydrogen peroxide [33,34].”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [33]
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Cites
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
REPAIR OF OXIDATIVE DAMAGE TO DNA: Enzymology and Biology
Demple, B., & Harrison, L. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.004411 · Cited by 1,495
New method for generating deletions and gene replacements in Escherichia coli
Hamilton, C. M., Aldea, M., Washburn, B. K., Babitzke, P., & Kushner, S. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.9.4617-4622.1989 · Cited by 678
Self-citationEnzymatic reduction of protein-bound methionine sulfoxide.
Brot, N., Weissbach, L., Werth, J. L., & Weissbach, H. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2155 · Cited by 359
Self-citationCochrane, C. G., Spragg, R. G., & Revak, S. D. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110823 · Cited by 356
Carp, H., Miller, F. W., Hoidal, J. R., & Janoff, A. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.2041 · Cited by 343
GENETIC BASIS OF STARVATION SURVIVAL IN NONDIFFERENTIATING BACTERIA
Matin, A., Auger, E. A., Blum, P., & Schultz, J. E. (1989) · Annual Review of Microbiology · doi:10.1146/annurev.mi.43.100189.001453 · Cited by 333
Selective oxidation of cysteine and methionine in normal and senile cataractous lenses.
Garner, M. H., & Spector, A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1274 · Cited by 301
Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival
Groat, R. G., Schultz, J. E., Zychlinsky, E., Bockman, A. T., & Matin, A. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.2.486-493.1986 · Cited by 264
Catalases HPI and HPII in Escherichia coli are induced independently
Loewen, P. C., Switala, J., & Triggs‐Raine, B. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90782-9 · Cited by 257
Oxidative changes in human lens proteins during senile nuclear cataract formation
Truscott, R. J. W., & Augusteyn, R. C. (1977) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(77)90212-4 · Cited by 254
Nucleotide sequence ofkatF ofEscherichia colisuggestsKatF protein is a novel σ transcription factor
Mulvey, M. R., & Loewen, P. C. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.23.9979 · Cited by 253
Willetts, N. S., & Mount, D. W. (1969) · Journal of Bacteriology · doi:10.1128/jb.100.2.923-934.1969 · Cited by 165
Aldea, M., Garrido, T., Hernández-Chico, C., Vicente, M., & Kushner, S. R. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08573.x · Cited by 164
Self-citationAn E. coli promoter induced by the cessation of growth
Connell, N. D., Han, Z., Moreno, F., & Kolter, R. (1987) · Molecular Microbiology · doi:10.1111/j.1365-2958.1987.tb00512.x · Cited by 134
Wong, P. S., & Travis, J. W. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)90113-8 · Cited by 129
Inactivation of plasminogen activator inhibitor by oxidants
Lawrence, D. A., & Loskutoff, D. J. (1986) · Biochemistry · doi:10.1021/bi00369a001 · Cited by 121
Biosynthesis of Bacterial Glycogen
Paule, M. R., & Preiss, J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62053-8 · Cited by 120
Okita, T. W., Rodriguez, R. L., & Preiss, J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69082-4 · Cited by 100
Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.
Abrams, W. R., Weinbaum, G., Weissbach, L., Weissbach, H., & Brot, N. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7483 · Cited by 97
Self-citationAmount and chain length of polyphosphates in Escherichia coli depend on cell growth conditions
Rao, N. N., Roberts, M. F., & Torriani, A. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.1.242-247.1985 · Cited by 81
Rahman, M. A., Nelson, H. R., Weissbach, H., & Brot, N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49570-7 · Cited by 75
Self-citationDassa, E., Cahu, M., Desjoyaux-Cherel, B., & Boquet, P. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34481-8 · Cited by 73
Growth phase and ompR regulation of transcription of microcin B17 genes
Hernández-Chico, C., Millán, J. L. S., Kolter, R., & Moreno, F. (1986) · Journal of Bacteriology · doi:10.1128/jb.167.3.1058-1065.1986 · Cited by 65
Tobler, P. H., Tschopp, F. A., Dambacher, M. A., Born, W., & Fischer, J. A. (1983) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-57-4-749 · Cited by 51
appR gene product activates transcription of microcin C7 plasmid genes
Díaz-Guerra, L., Moreno, F., & Millán, J. L. S. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2906-2908.1989 · Cited by 47
Biosynthesis of bacterial glycogen
Preiss, J., Lammel, C. J., & Greenberg, E. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90329-5 · Cited by 35
Oxidation of alpha 1-protease inhibitor: role of lipid peroxidation products
Mohsenin, V., & Gee, J. L. (1989) · Journal of Applied Physiology · doi:10.1152/jappl.1989.66.5.2211 · Cited by 27
Fliss, H., Vasanthakumar, G., Schiffmann, E., Weissbach, H., & Brot, N. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91584-4 · Cited by 19
Self-citationMethionine Sulfoxide: Chemistry and Biochemistry
Brot, N., & Weissbach, H. (2006) · Wiley eBooks · doi:10.1002/0470034386.ch17 · Cited by 14
Self-citationRahman, M. A., Brot, N., & Weissbach, H. (1992) · PubMed · Cited by 11
Self-citation
Research works printed but not linked: 1
- Ausubel F. M. R. Brent R. E. Kingston D. D. Moore J. G. Seidman J. A. Smith and K. Struhl (ed.). 1989. Current protocols in molecular biology. Greene Publishing Associates and Wiley-Interscience New York.
Cited by
Sorted by citations
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563
Storz, G., & Imlayt, J. A. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80033-2 · Cited by 1,077
Stadtman, E. R. (2006) · Free Radical Research · doi:10.1080/10715760600918142 · Cited by 1,056
Oxidative stress, protein damage and repair in bacteria
Ezraty, B., Gennaris, A., Barras, F., & Collet, J. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.26 · Cited by 1,042
Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease
Stadtman, E. R., & Berlett, B. S. (1998) · Drug Metabolism Reviews · doi:10.3109/03602539808996310 · Cited by 899
Metadata
- Authors
- Moskovitz, J., Rahman, M. A., Strassman, J., Yancey, S. O., Kushner, S. R., Brot, N., & Weissbach, H.
- Affiliations
- Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1995-02
- Volume
- 177
- Issue
- 3
- Pages
- 502-507
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC176620
- OpenAlex
- W2107508146
- Cited by
- 294
- References
- 31
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 5 · 2021: 7 · 2020: 4 · 2019: 9 · 2018: 8 · 2017: 4 · 2016: 9 · 2015: 9 · 2014: 3 · 2013: 10 · 2012: 7
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (University of Kansas) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- Escherichia coli, msrA gene, methionine sulfoxide reductase, gene expression regulation, promoter analysis, transcription start sites, oxidative stress sensitivity, oxidative damage protection
- MeSH terms
- Base Sequence, Escherichia coli, Genes, Bacterial, Methionine, Molecular Sequence Data, Mutation, Oxidoreductases, RNA, Messenger, Gene Expression Regulation, Bacterial, Oxidative Stress, Methionine Sulfoxide Reductases
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