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Selective Inhibition of Selenocysteine tRNA Maturation and Selenoprotein Synthesis in Transgenic Mice Expressing Isopentenyladenosine-Deficient Selenocysteine tRNA
Open accessAbstract
Selenocysteine (Sec) tRNA (tRNA([Ser]Sec)) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein biosynthesis of overexpressing either the wild type or a mutant tRNA([Ser]Sec) lacking the modified base, isopentenyladenosine, in its anticodon loop were examined by introducing multiple copies of the corresponding tRNA([Ser]Sec) genes into the mouse genome. Overexpression of wild-type tRNA([Ser]Sec) did not affect selenoprotein synthesis. In contrast, the levels of numerous selenoproteins decreased in mice expressing isopentenyladenosine-deficient (i(6)A(-)) tRNA([Ser]Sec) in a protein- and tissue-specific manner. Cytosolic glutathione peroxidase and mitochondrial thioredoxin reductase 3 were the most and least affected selenoproteins, while selenoprotein expression was most and least affected in the liver and testes, respectively. The defect in selenoprotein expression occurred at translation, since selenoprotein mRNA levels were largely unaffected. Analysis of the tRNA([Ser]Sec) population showed that expression of i(6)A(-) tRNA([Ser]Sec) altered the distribution of the two major isoforms, whereby the maturation of tRNA([Ser]Sec) by methylation of the nucleoside in the wobble position was repressed. The data suggest that the levels of i(6)A(-) tRNA([Ser]Sec) and wild-type tRNA([Ser]Sec) are regulated independently and that the amount of wild-type tRNA([Ser]Sec) is determined, at least in part, by a feedback mechanism governed by the level of the tRNA([Ser]Sec) population. This study marks the first example of transgenic mice engineered to contain functional tRNA transgenes and suggests that i(6)A(-) tRNA([Ser]Sec) transgenic mice will be useful in assessing the biological roles of selenoproteins.
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“The transcription factor Nrf2 is considered as a redox switch regulating the expression of antioxidant enzymes, GSH-synthesizing enzymes, and detoxifying Phase 2 enzymes (175), while the specific selenocysteine tRNA is needed for the synthesis of selenoproteins such as GPx or Trx reductase, which reduces oxidized Trx (133) (Fig. 2).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [133]
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Cites
A simple salting out procedure for extracting DNA from human nucleated cells
Miller, S. A., Dykes, D. D., & Polesky, H. F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.3.1215 · Cited by 20,341
Glutathione peroxidase activity in selenium-deficient rat liver
Lawrence, R. A., & Burk, R. F. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90747-6 · Cited by 3,536
Self-citationComprehensive natural products chemistry
(1999) · Choice Reviews Online · doi:10.5860/choice.37-0939 · Cited by 1,621
Factors affecting the efficiency of introducing foreign DNA into mice by microinjecting eggs.
Brinster, R. L., Chen, H. Y., Trumbauer, M. E., Yagle, M. K., & Palmiter, R. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4438 · Cited by 1,028
Ganther, H. E. (1999) · Carcinogenesis · doi:10.1093/carcin/20.9.1657 · Cited by 690
Modification and Editing of RNA
Auffinger, P., Grosjean, H., & Benne, R. (1998) · ASM Press eBooks · doi:10.1128/9781555818296 · Cited by 643
Evidence for specific selenium target tissues and new biologically important selenoproteins
BEHNE, D., Hilmert, H., Scheid, S., Gessner, H., & Elger, W. A. G. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90123-7 · Cited by 466
Knowing when not to stop: selenocysteine incorporation in eukaryotes
Low, S. C., & Berry, M. J. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)80016-8 · Cited by 449
Self-citationIp, C. C. Y., Thompson, H. J., Zhu, Z., & Ganther, H. E. (2000) · PubMed · Cited by 413
A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
Copeland, P. R., Fletcher, J. E., Carlson, B. A., Hatfield, D. L., & Driscoll, D. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.2.306 · Cited by 398
Self-citation
Research works printed but not linked: 7
- Bjork G. R., 1998, Modification and editing of RNA., 471
- Curran J. F., 1998, Modification and editing of tRNA., 493
- Gladyshev V. N., 1999, Recent Res. Dev. Biochem., 1, 145
- Ip C., 2000, Cancer Res., 60, 2882
- Lee B. J., 1990, Mol. Cell. Biol., 10, 1940
- Lei X. G., 1995, J. Nutr., 125, 1438
- Ohama T., 1995, Biochem. Mol. Biol. Int., 36, 421
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Doyle, F., Leonardi, A., Endres, L., Tenenbaum, S. A., Dedon, P. C., & Begley, T. J. (2016) · Methods · doi:10.1016/j.ymeth.2016.05.010 · Cited by 28
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Self-citationWang, S. K., Weaver, J. D., Zhang, S., & Lei, X. G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.018 · Cited by 28
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Selenium, a versatile trace element: current research implications.
Bansal, M. P., & Kaur, P. (2005) · PubMed · Cited by 27
Selenocysteine tRNA methylation promotes oxidative stress resistance in melanoma metastasis
Nease, L. A., Church, K. P., Delclaux, I., Murakami, S., Astorkia, M., Zerhouni, M., Cascio, G., Hughes, R. O., Aguirre, K. N., Zumbo, P., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00844-8 · Cited by 25
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Self-citationIodothyronine deiodinases and cancer.
Piekiełko‐Witkowska, A., & Nauman, A. (2011) · PubMed · doi:10.3275/7754 · Cited by 24
Xu, X.-M., Carlson, B. A., Grimm, T. A., Kutza, J., Berry, M. J., Arreola, R., Fields, K. H., Shanmugam, I., Jeang, K., Oroszlan, S. I., et al. (2002) · JAIDS Journal of Acquired Immune Deficiency Syndromes · doi:10.1097/00126334-200212150-00001 · Cited by 21
Self-citationSimonović, M., & Puppala, A. K. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.018 · Cited by 22
Kelly, V. P., Suzuki, T., Nakajima, O., Arai, T., Tamai, Y., Takahashi, S., Nishimura, S., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3658-3669.2005 · Cited by 20
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Jameson, R. R., Butz, M., Diamond, A. M., Carlson, B. A., Esser, K. A., & Hatfield, D. L. (2002) · Journal of Nutrition · doi:10.1093/jn/132.7.1830 · Cited by 20
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Johansson, L., Svensson, L., Bergström, U., Jacobsson‐Ekman, G., Arnér, E. S. J., van Hage, M., Bucht, A., & Gafvelin, G. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04764.x · Cited by 17
Carlson, B. A., Xu, X., Gladyshev, V. N., & Hatfield, D. L. (2005) · Topics in current genetics · doi:10.1007/b106652 · Cited by 16
Self-citationMahdi, Y., Xu, X.-M., Carlson, B. A., Fradejas‐Villar, N., Günter, P., Braun, D., Southon, E. A., Tessarollo, L., Hatfield, D. L., & Schweizer, U. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127349 · Cited by 15
Self-citationSantoro, A., Ciaglia, E., Nicolin, V., Pescatore, A., Prota, L., Capunzo, M., Ursini, M. V., Nori, S. L., & Bifulco, M. (2017) · Inflammation Research · doi:10.1007/s00011-017-1123-6 · Cited by 16
Transfer RNAs That Insert Selenocysteine
Carlson, B. A., & Hatfield, D. L. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)47005-x · Cited by 16
Self-citation
Metadata
- Authors
- Moustafa, M. E., Carlson, B. A., El-Saadani, M. A., Kryukov, G. V., Sun, Q.-A., Harney, J. W., Hill, K. E., Combs, G. F., Feigenbaum, L., Mansur, D. B., Burk, R. F., Berry, M. J., Diamond, A. M., Lee, B. J., Gladyshev, V. N., & Hatfield, D. L.
- Affiliations
- National Institutes of Health (US)
- Alexandria University (EG)
- University of Nebraska–Lincoln (US)
- Brigham and Women's Hospital (US)
- Vanderbilt University (US)
- Cornell University (US)
- Leidos (United States) (US)
- Washington University in St. Louis (US)
- University of Illinois Chicago (US)
- Seoul National University (KR)
- ORCID
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2001-06-01
- Volume
- 21
- Issue
- 11
- Pages
- 3840-3852
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC87048
- OpenAlex
- W2141386840
- Cited by
- 131
- References
- 47
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 5 · 2023: 3 · 2021: 5 · 2019: 2 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 6 · 2012: 4
- FWCI
- 6.72
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lincoln (University of Nebraska) (submittedVersion)
- Funders
- American Institute for Cancer Research
- National Institutes of Health (DK47320, ES02497)
- National Cancer Institute (CAA81153)
- National Institute of General Medical Sciences (GM616603)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 47320, R56DK047320, R01DK047320)
- National Institute of Environmental Health Sciences (ES-02497, R37ES002497, R01ES002497)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
- Keywords
- selenocysteine tRNA, selenoprotein biosynthesis, isopentenyladenosine, tRNA maturation, glutathione peroxidase, transgenic mice, feedback regulation, anticodon loop, tissue-specific gene expression
- MeSH terms
- Animals, Base Sequence, Isopentenyladenosine, Mice, Transgenic, Molecular Sequence Data, Nucleic Acid Conformation, Proteins, RNA, Transfer, Amino Acid-Specific, Selenium, Protein Biosynthesis, Blotting, Northern, Gene Expression, Selenoproteins, Mice
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