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Titolo:
Eukaryotic selenocysteine incorporation follows a nonprocessive mechanism that competes with translational termination
Autore:
Nasim, MT; Jaenecke, S; Belduz, A; Kollmus, H; Flohe, L; McCarthy, JEG;
Indirizzi:
Univ Manchester, Dept Biomol Sci, Postranscript Control Grp, Manchester M60 1QD, Lancs, England Univ Manchester Manchester Lancs England M60 1QD M60 1QD, Lancs, England Tech Univ Braunschweig, Dept Biochem, D-38124 Braunschweig, Germany Tech Univ Braunschweig Braunschweig Germany D-38124 raunschweig, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 20, volume: 275, anno: 2000,
pagine: 14846 - 14852
SICI:
0021-9258(20000519)275:20<14846:ESIFAN>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYDROPEROXIDE GLUTATHIONE-PEROXIDASE; INSERTION-SEQUENCE ELEMENT; MESSENGER-RNA STABILITY; SELENOPROTEIN SYNTHESIS; COTRANSLATIONAL INCORPORATION; FUNCTIONAL-CHARACTERIZATION; ESCHERICHIA-COLI; BINDING PROTEIN; XENOPUS-LAEVIS; AMINO-ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: McCarthy, JEG Univ Manchester, Dept Biomol Sci, Postranscript Control Grp,POB 88, Manchester M60 1QD, Lancs, England Univ Manchester POB 88 Manchester Lancs England M60 1QD land
Citazione:
M.T. Nasim et al., "Eukaryotic selenocysteine incorporation follows a nonprocessive mechanism that competes with translational termination", J BIOL CHEM, 275(20), 2000, pp. 14846-14852

Abstract

The synthesis of eukaryotic selenoproteins involves the recoding of an internal UGA codon as a site for selenocysteine incorporation. This recoding event is directed by a selenocysteine insertion sequence in the 3'-untranslated region. Because UGA also functions as a signal for peptidyl-tRNA hydrolysis, we have investigated how the rates of translational termination and selenocysteine incorporation relate to cia-acting elements in the mRNA as well as to trans-acting factors in the cytoplasm, We used cia-elements from the phospholipid glutathione peroxidase gene as the basis for this work because of its relatively high efficiency of selenocysteine incorporation. The last two codons preceding the UGA were found to exert a far greater influence on selenocysteine incorporation than nucleotides downstream of it, The efficiency of selenocysteine incorporation was generally much less than 100%but could be partially enhanced by concomitant overexpression of the tRNA(Sec) gene. The combination of two or three UGA codons in one reading frame led to a dramatic reduction in the yield of full-length protein. It is therefore unlikely that multiple incorporations of selenocysteine are processive with respect to the mode of action of the ribosomal complex binding to the UGA site. These observations are discussed in terms of the mechanism of selenoprotein synthesis and its ability to compete with termination at UGA codons.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 21:50:57