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Titolo:
Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms
Autore:
Lundberg, M; Johansson, C; Chandra, J; Enoksson, M; Jacobsson, G; Ljung, J; Johansson, M; Holmgren, A;
Indirizzi:
Karolinska Inst, Med Nobel Inst Biochem, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17177 phys, S-17177 Stockholm, Sweden Karolinska Inst, Inst Environm Med, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17177 Med, S-17177 Stockholm, Sweden Karolinska Hosp, Dept Med, Unit Clin Allergy Res, S-17176 Stockholm, Sweden Karolinska Hosp Stockholm Sweden S-17176 Res, S-17176 Stockholm, Sweden Huddinge Univ, Div Clin Virol, S-14186 Huddinge, Sweden Huddinge Univ Huddinge Sweden S-14186 in Virol, S-14186 Huddinge, Sweden
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 28, volume: 276, anno: 2001,
pagine: 26269 - 26275
SICI:
0021-9258(20010713)276:28<26269:CAEOAN>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI GLUTAREDOXIN; PROTEIN DISULFIDE-ISOMERASE; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; GLUTATHIONE-DEPENDENT SYNTHESIS; OXYR TRANSCRIPTION FACTOR; HYDROGEN DONOR SYSTEM; HIGH-LEVEL EXPRESSION; DNA-BINDING ACTIVITY; AMINO-ACID-SEQUENCE; THIOLTRANSFERASE GLUTAREDOXIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Holmgren, A Karolinska Inst, Med Nobel Inst Biochem, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-171777 Stockholm, Sweden
Citazione:
M. Lundberg et al., "Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms", J BIOL CHEM, 276(28), 2001, pp. 26269-26275

Abstract

Glutaredoxin (Grx) is a glutathione-dependent hydrogen donor for ribonucleotide reductase, Today glutaredoxins are known as a multifunctional family of GSH-disulfide-oxidoreductases belonging to the thioredoxin fold superfamily, In contrast to Escherichia coli and yeast, a single human glutaredoxinis known. We have identified and cloned a novel 18-kDa human dithiol glutaredoxin, named glutaredoxin-2 (Grx2), which is 34% identical to the previously known cytosolic 12-kDa human Grx1. The human Grx2 sequence contains three characteristic regions of the glutaredoxin family: the dithiol/disulfideactive site, CSYC, the GSH binding site, and a hydrophobic surface area. The human Grx2 gene, located at chromosome 1q31.2-31.3, consisted of five exons that were transcribed to a 0.9-kilobase human Grx2 mRNA ubiquitously expressed in several tissues. Two alternatively spliced Grx2 mRNA isoforms that differed in their 5 ' region were identified. These corresponded to alternative proteins with a common 125-residue C-terminal Grx domain but with different N-terminal extensions of 39 and 40 residues, respectively. The 125-residue Grx domain and the two full-length variants were expressed in E. coli and exhibited GSH-dependent hydroxyethyl disulfide and dehydroascorbatereducing activities. Western blot analysis of subcellular fractions from Jurkat cells with a specific anti-Grx2 antibody showed that human Grx2 was predominantly located in the nucleus but also present in the mitochondria, We further showed that one of the mRNA isoforms corresponding to Grx2a encoded a functional N-terminal mitochondrial translocation signal.

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Documento generato il 30/11/20 alle ore 07:09:06