Serveur d'exploration sur la glutarédoxine

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A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.

Identifieur interne : 001041 ( Main/Exploration ); précédent : 001040; suivant : 001042

A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.

Auteurs : M. Mazzocco [Italie] ; P. Arrigo ; A. Egeo ; M. Maffei ; A. Vergano ; R. Di Lisi ; F. Ghiotto ; E. Ciccone ; R. Cinti ; R. Ravazzolo ; P. Scartezzini

Source :

RBID : pubmed:11444877

Descripteurs français

English descriptors

Abstract

Glutaredoxins (GRXs) are ubiquitous GSH-dependent oxidoreductases, which catalyze the reduction of protein-glutathionyl-mixed disulfides and are considered to play an important role in the enzymatic regulation of redox-sensitive proteins. In this paper, we describe the identification and characterization of a new human homologue of the SH3BGR gene, named SH3BGRL3 (SH3 domain binding glutamic acid-rich protein like 3). SH3BGRL3 is widely expressed and codes for a highly conserved small protein, which shows a significant similarity to Glutaredoxin 1 (GRX1) of Escherichia coli and is predicted to belong to the Thioredoxin Superfamily. However, the SH3BGRL3 protein lacks both the conserved cysteine residues, which characterize the enzymatic active site of GRX. This structural feature raises the possibility that SH3BGRL3 could function as an endogenous modulator of GRX biological activity. EGFP-SH3BGRL3 fusion protein expressed in COS-7 cells localizes both to the nucleus and to the cytoplasm. The SH3BGRL3 gene was mapped to chromosome 1p34.3-35.

DOI: 10.1006/bbrc.2001.5169
PubMed: 11444877


Affiliations:


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Le document en format XML

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<term>Bacterial Proteins (genetics)</term>
<term>Base Sequence (MeSH)</term>
<term>COS Cells (MeSH)</term>
<term>Cell Line (MeSH)</term>
<term>Chlorocebus aethiops (MeSH)</term>
<term>Chromosome Mapping (MeSH)</term>
<term>Chromosomes, Human, Pair 1 (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Conserved Sequence (MeSH)</term>
<term>Escherichia coli (genetics)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Jurkat Cells (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Muscle Proteins (chemistry)</term>
<term>Muscle Proteins (genetics)</term>
<term>Organ Specificity (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Proteins (chemistry)</term>
<term>Proteins (genetics)</term>
<term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>T-Lymphocytes (MeSH)</term>
<term>Thioredoxins (chemistry)</term>
<term>Thioredoxins (genetics)</term>
<term>Transcription, Genetic (MeSH)</term>
<term>Transfection (MeSH)</term>
<term>Tumor Cells, Cultured (MeSH)</term>
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<term>Animaux (MeSH)</term>
<term>Cartographie chromosomique (MeSH)</term>
<term>Cellules COS (MeSH)</term>
<term>Cellules Jurkat (MeSH)</term>
<term>Cellules cancéreuses en culture (MeSH)</term>
<term>Chromosomes humains de la paire 1 (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
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<term>Glutarédoxines (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Lymphocytes T (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
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<term>Protéines (génétique)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (génétique)</term>
<term>Protéines du muscle (composition chimique)</term>
<term>Protéines du muscle (génétique)</term>
<term>RT-PCR (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Souris (MeSH)</term>
<term>Spécificité d'organe (MeSH)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Thiorédoxines (composition chimique)</term>
<term>Thiorédoxines (génétique)</term>
<term>Transcription génétique (MeSH)</term>
<term>Transfection (MeSH)</term>
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<term>Bacterial Proteins</term>
<term>Muscle Proteins</term>
<term>Proteins</term>
<term>Thioredoxins</term>
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<term>Bacterial Proteins</term>
<term>Muscle Proteins</term>
<term>Proteins</term>
<term>Thioredoxins</term>
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<term>Protéines</term>
<term>Protéines bactériennes</term>
<term>Protéines du muscle</term>
<term>Thiorédoxines</term>
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<term>Escherichia coli</term>
<term>Protéines</term>
<term>Protéines bactériennes</term>
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<term>Thiorédoxines</term>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Base Sequence</term>
<term>COS Cells</term>
<term>Cell Line</term>
<term>Chlorocebus aethiops</term>
<term>Chromosome Mapping</term>
<term>Chromosomes, Human, Pair 1</term>
<term>Cloning, Molecular</term>
<term>Conserved Sequence</term>
<term>Glutaredoxins</term>
<term>Humans</term>
<term>Jurkat Cells</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
<term>Organ Specificity</term>
<term>Oxidoreductases</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
<term>Sequence Alignment</term>
<term>Sequence Homology, Amino Acid</term>
<term>T-Lymphocytes</term>
<term>Transcription, Genetic</term>
<term>Transfection</term>
<term>Tumor Cells, Cultured</term>
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<term>Animaux</term>
<term>Cartographie chromosomique</term>
<term>Cellules COS</term>
<term>Cellules Jurkat</term>
<term>Cellules cancéreuses en culture</term>
<term>Chromosomes humains de la paire 1</term>
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<term>Données de séquences moléculaires</term>
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<term>Similitude de séquences d'acides aminés</term>
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<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
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<front>
<div type="abstract" xml:lang="en">Glutaredoxins (GRXs) are ubiquitous GSH-dependent oxidoreductases, which catalyze the reduction of protein-glutathionyl-mixed disulfides and are considered to play an important role in the enzymatic regulation of redox-sensitive proteins. In this paper, we describe the identification and characterization of a new human homologue of the SH3BGR gene, named SH3BGRL3 (SH3 domain binding glutamic acid-rich protein like 3). SH3BGRL3 is widely expressed and codes for a highly conserved small protein, which shows a significant similarity to Glutaredoxin 1 (GRX1) of Escherichia coli and is predicted to belong to the Thioredoxin Superfamily. However, the SH3BGRL3 protein lacks both the conserved cysteine residues, which characterize the enzymatic active site of GRX. This structural feature raises the possibility that SH3BGRL3 could function as an endogenous modulator of GRX biological activity. EGFP-SH3BGRL3 fusion protein expressed in COS-7 cells localizes both to the nucleus and to the cytoplasm. The SH3BGRL3 gene was mapped to chromosome 1p34.3-35.</div>
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<AbstractText>Glutaredoxins (GRXs) are ubiquitous GSH-dependent oxidoreductases, which catalyze the reduction of protein-glutathionyl-mixed disulfides and are considered to play an important role in the enzymatic regulation of redox-sensitive proteins. In this paper, we describe the identification and characterization of a new human homologue of the SH3BGR gene, named SH3BGRL3 (SH3 domain binding glutamic acid-rich protein like 3). SH3BGRL3 is widely expressed and codes for a highly conserved small protein, which shows a significant similarity to Glutaredoxin 1 (GRX1) of Escherichia coli and is predicted to belong to the Thioredoxin Superfamily. However, the SH3BGRL3 protein lacks both the conserved cysteine residues, which characterize the enzymatic active site of GRX. This structural feature raises the possibility that SH3BGRL3 could function as an endogenous modulator of GRX biological activity. EGFP-SH3BGRL3 fusion protein expressed in COS-7 cells localizes both to the nucleus and to the cytoplasm. The SH3BGRL3 gene was mapped to chromosome 1p34.3-35.</AbstractText>
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   |wiki=    Bois
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   |texte=   A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.
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