Knowing when not to stop: selenocysteine incorporation in eukaryotes - PubMed (original) (raw)
Affiliations
- PMID: 8744353
Knowing when not to stop: selenocysteine incorporation in eukaryotes
S C Low et al. Trends Biochem Sci. 1996 Jun.
Abstract
The regulation of translation frequently involves protein-RNA interactions. An intriguing example of this is the alternative decoding of UGA, typically a stop codon, as selenocysteine. Two RNA structures, the mRNA selenocysteine insertion sequence (SECIS element) and a unique selenocysteyl-tRNA, are required for this process. In prokaryotes, a single RNA-binding protein, a selenocysteine-specific elongation factor, interacts with both the tRNA and mRNA to confer decoding. Whether eukaryotes use a similar mechanism is currently the subject of intense investigation.
Similar articles
- Decoding apparatus for eukaryotic selenocysteine insertion.
Tujebajeva RM, Copeland PR, Xu XM, Carlson BA, Harney JW, Driscoll DM, Hatfield DL, Berry MJ. Tujebajeva RM, et al. EMBO Rep. 2000 Aug;1(2):158-63. doi: 10.1093/embo-reports/kvd033. EMBO Rep. 2000. PMID: 11265756 Free PMC article. - [Selenoproteins--atypical function of the UGA codon].
Rybka K. Rybka K. Postepy Hig Med Dosw. 1999;53(4):601-16. Postepy Hig Med Dosw. 1999. PMID: 10544661 Review. Polish. - Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes.
Chavatte L, Brown BA, Driscoll DM. Chavatte L, et al. Nat Struct Mol Biol. 2005 May;12(5):408-16. doi: 10.1038/nsmb922. Epub 2005 Apr 10. Nat Struct Mol Biol. 2005. PMID: 15821744 - Eukaryotic selenoprotein synthesis: mechanistic insight incorporating new factors and new functions for old factors.
Squires JE, Berry MJ. Squires JE, et al. IUBMB Life. 2008 Apr;60(4):232-5. doi: 10.1002/iub.38. IUBMB Life. 2008. PMID: 18344183 Review. - Interplay between termination and translation machinery in eukaryotic selenoprotein synthesis.
Grundner-Culemann E, Martin GW 3rd, Tujebajeva R, Harney JW, Berry MJ. Grundner-Culemann E, et al. J Mol Biol. 2001 Jul 20;310(4):699-707. doi: 10.1006/jmbi.2001.4809. J Mol Biol. 2001. PMID: 11453681
Cited by
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.
Jann C, Giofré S, Bhattacharjee R, Lemke EA. Jann C, et al. Chem Rev. 2024 Sep 25;124(18):10281-10362. doi: 10.1021/acs.chemrev.3c00878. Epub 2024 Aug 9. Chem Rev. 2024. PMID: 39120726 Review. - Expression levels of the selenium-uptake receptor LRP8, the antioxidant selenoprotein GPX1 and steroidogenic enzymes correlate in granulosa cells.
Hummitzsch K, Kelly JE, Hatzirodos N, Bonner WM, Tang F, Harris HH, Rodgers RJ. Hummitzsch K, et al. Reprod Fertil. 2024 Aug 2;5(3):e230074. doi: 10.1530/RAF-23-0074. Print 2024 Jul 1. Reprod Fertil. 2024. PMID: 38990713 Free PMC article. - Molecular characterization and expression analysis of selenoprotein W gene in rainbow trout (Oncorhynchus mykiss) with dietary selenium levels.
Liao C, Zhang F, Teng Z, Zhang G, Yang Y, Xu P, Huang X, Wang L, Yang F, Yang Z, Zhang X. Liao C, et al. Biometals. 2022 Dec;35(6):1359-1370. doi: 10.1007/s10534-022-00451-z. Epub 2022 Oct 20. Biometals. 2022. PMID: 36261677 - Reactive Human Plasma Glutathione Peroxidase Mutant with Diselenide Bond Succeeds in Tetramer Formation.
Fan Z, Yan Q, Song J, Wei J. Fan Z, et al. Antioxidants (Basel). 2022 May 29;11(6):1083. doi: 10.3390/antiox11061083. Antioxidants (Basel). 2022. PMID: 35739980 Free PMC article. - Comparative Proteomic Analysis Reveals the Effect of Selenoprotein W Deficiency on Oligodendrogenesis in Fear Memory.
Situ J, Huang X, Zuo M, Huang Y, Ren B, Liu Q. Situ J, et al. Antioxidants (Basel). 2022 May 19;11(5):999. doi: 10.3390/antiox11050999. Antioxidants (Basel). 2022. PMID: 35624863 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources