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A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2001 Jul 13; Vol. 285 (2), pp. 540-5. - Publication Year :
- 2001
-
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.<br /> (Copyright 2001 Academic Press.)
- Subjects :
- Amino Acid Sequence
Animals
Bacterial Proteins chemistry
Bacterial Proteins genetics
Base Sequence
COS Cells
Cell Line
Chlorocebus aethiops
Chromosome Mapping
Cloning, Molecular
Conserved Sequence
Glutaredoxins
Humans
Jurkat Cells
Mice
Molecular Sequence Data
Muscle Proteins chemistry
Organ Specificity
Proteins chemistry
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Homology, Amino Acid
T-Lymphocytes
Thioredoxins chemistry
Thioredoxins genetics
Transcription, Genetic
Transfection
Tumor Cells, Cultured
Chromosomes, Human, Pair 1
Escherichia coli genetics
Muscle Proteins genetics
Oxidoreductases
Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 285
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 11444877
- Full Text :
- https://doi.org/10.1006/bbrc.2001.5169