The genes (selC) coding for the selenocysteine-inserting tRNA species (tRNA(Sec)) from Clostridium thermoaceticum and Desulfomicrobium baculatum were cloned and sequenced. Although they differ in numerous positions from the sequence of the Escherichia coli selC gene, they were able to complement the selC lesion of an E. coli mutant and to promote selenoprotein formation in the heterologous host. The tRNA(Sec) species from both organisms possess all of the unique primary, secondary, and tertiary structural features exhibited by E. coli tRNA(Sec) (C. Baron, E. Westhof, A. Böck, and R. Giegé, J. Mol. Biol. 231:274-292, 1993). The structural and functional properties of the tRNA(Sec) species from prokaryotes analyzed thus far support the notion that tRNA(Sec) may be an evolutionarily conserved structure whose function in the primordial genetic code was to decode UGA with selenocysteine.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC205188 | PMC |
http://dx.doi.org/10.1128/jb.176.5.1268-1274.1994 | DOI Listing |
Biol Chem
January 2003
German Institute of Human Nutrition, Department of Vitamins and Atherosclerosis, D-14558 Potsdam-Rehbrücke, Germany.
Selenoprotein mRNAs are particular in several aspects. They contain a specific secondary structure in their 3'UTR, called Secis (selenocysteine inserting sequence), which is indispensable for selenocysteine incorporation, and they are degraded under selenium-limiting conditions according to their ranking in the hierarchy of selenoproteins. In the familiy of selenium-dependent glutathione peroxidases (GPx) the ranking is GI-GPx > or = PHGPx > cGPx = pGPx.
View Article and Find Full Text PDFJ Biol Chem
April 1998
Section on the Molecular Biology of Selenium, Basic Research Laboratory, NCI, National Institutes of Health, Bethesda, Maryland 20892,
Selenium which occurs in proteins as the amino acid, selenocysteine, is essential for numerous biological processes and for human health. A prominent 75Se-labeled protein detected in human T-cells migrated as a 15-kDa band by SDS-polyacrylamide gel electrophoresis. This protein subunit was purified and subjected to tryptic digestion and peptide sequence analyses.
View Article and Find Full Text PDFZ Ernahrungswiss
May 1998
National Biotechnology Research Centre (GBF), Braunschweig, Germany.
A convenient test system was designed to investigate the efficiencies of selenocysteine inserting sequences (SECIS) responsible for the cotranslational incorporation of selenocysteine into selenoproteins of mammals. It comprises an expression vector in which the lacZ and luc genes are separated by an in-frame TGA stop codon. The coding regions are followed by a multicloning region allowing exchange of putative SECIS elements.
View Article and Find Full Text PDFBiofactors
October 1997
GBF-National Research Centre for Biotechnology, Braunschweig, Germany.
An 11-day embryonic Swiss Webster/NIH mouse cDNA library was screened with a partial murine selenoprotein P cDNA probe and a murine selenoprotein-P-type cDNA clone of 2075 bp length was obtained. The clone contained a 5'-leader sequence of 132 bp length, the selenoprotein P coding frame, and 803 base pairs in the 3' untranslated region. Alignment and RNA folding studies revealed the presence of two well conserved selenocysteine inserting motifs in the 3' flanking region.
View Article and Find Full Text PDFJ Bacteriol
March 1994
Lehrstuhl für Mikrobiologie, Universität München, Germany.
The genes (selC) coding for the selenocysteine-inserting tRNA species (tRNA(Sec)) from Clostridium thermoaceticum and Desulfomicrobium baculatum were cloned and sequenced. Although they differ in numerous positions from the sequence of the Escherichia coli selC gene, they were able to complement the selC lesion of an E. coli mutant and to promote selenoprotein formation in the heterologous host.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!