Alternative forms of the human thioredoxin mRNA: identification and characterization

Gene
J HariharanS Datta

Abstract

Thioredoxin (TRX) is an ubiquitous and relatively conserved oxidoreductant enzyme which is involved in a multitude of redox reactions through the formation of reversible disulfide bonds. A recent report indicates the presence of novel isoforms of TRX proteins isolated from MP6 cell lines [Rosén et al., Int. Immunol. 7 (1995) 625-633]. In these isoforms, as evidenced from amino acid sequencing, several Lys residues of the wild-type sequence were replaced by Arg. Although the human genome contains several (isoformic) copies of the TRX gene, only one appears to be transcriptionally active [Kaghad et al., Gene, 140 (1994) 273-278]. As we characterized the isoforms of TRX mRNAs, we found that several MP6 TRX cDNA clones were devoid of the characteristic poly(A) tail. In order to increase the efficiency of isolating mRNAs without the poly(A) tail, we developed a novel procedure for exclusive capturing of a specific mRNA by magnetic beads coated with biotinylated antisense oligodeoxyribonucleotide. Using this method on MP6 cell total RNA, we isolated an additional truncated version of the TRX mRNA. This latter form does not produce any variant TRX enzyme, as an inframe stop codon truncates the product. This isoform was also present in...Continue Reading

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Citations

Mar 24, 2004·Biochemical Pharmacology·Kerstin Jönsson-VidesäterMikael Björnstedt
Oct 18, 2000·Free Radical Biology & Medicine·G PowisA Coon
Feb 25, 2003·Protein Expression and Purification·Alberto Jiménez, Antonio Miranda-Vizuete
Dec 21, 2007·Antioxidants & Redox Signaling·Maria Elisabet LönnChristopher Horst Lillig
Nov 23, 2006·Antioxidants & Redox Signaling·Christopher Horst Lillig, Arne Holmgren
Mar 27, 2001·Annual Review of Pharmacology and Toxicology·G Powis, W R Montfort
Jul 10, 2001·Annual Review of Biophysics and Biomolecular Structure·G Powis, W R Montfort

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