These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Characterization of selenium-containing tRNAGlu from Clostridium sticklandii. Author: Ching WM. Journal: Arch Biochem Biophys; 1986 Jan; 244(1):137-46. PubMed ID: 2418784. Abstract: A selenium-containing tRNA from Clostridium sticklandii has been shown to be an isoaccepting tRNAGlu (W.-M. Ching and T. C. Stadtman (1982) Proc. Natl. Acad. Sci. USA 79, 374-377). Not only is this tRNAGlu one of the most abundant selenium-containing tRNA species but it is also the major glutamate isoacceptor in this organism. The selenonucleoside, which is located at the first position of the anticodon, was identified as 5-methylaminomethyl-2-selenouridine (A. J. Wittwer, L. Tsai, W.-M. Ching, and T. C. Stadt (1984) Biochemistry 23, 4650-4655). Other modified nucleosides present in this tRNA include 4-thiouridine, pseudouridine, ribothymidine, modified guanosine, and two different modified adenosines. When this seleno-tRNAGlu is incubated in 1.0 M Tris X HCl, pH 8.5, partial deselenization occurs. Moreover, treatment with cyanogen bromide almost completely removes the selenium. The presence of selenium in this tRNAGlu is essential for its enzymatic acylation with glutamate. This seleno-tRNAGlu recognizes both GAA and GAG codons. However, at 10 mM magnesium, which is near the physiological range, the GAA codon is slightly favored. In a cell free translation system, the acylated seleno-tRNAGlu is a very active glutamate donor.[Abstract] [Full Text] [Related] [New Search]