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 served 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.
| Original language | English |
|---|---|
| Pages (from-to) | 540-545 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 285 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2001 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A novel human homologue of the SH3BGR gene encodes a small protein similar to glutaredoxin 1 of Escherichia coli. / Mazzocco, M.; Arrigo, P.; Egeo, A.; Maffei, M.; Vergano, A.; Di Lisi, R.; Ghiotto, F.; Ciccone, E.; Cinti, R.; Ravazzolo, R.; Scartezzini, P.
In: Biochemical and Biophysical Research Communications, Vol. 285, No. 2, 2001, p. 540-545.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A novel human homologue of the SH3BGR gene encodes a small protein similar to glutaredoxin 1 of Escherichia coli
AU - Mazzocco, M.
AU - Arrigo, P.
AU - Egeo, A.
AU - Maffei, M.
AU - Vergano, A.
AU - Di Lisi, R.
AU - Ghiotto, F.
AU - Ciccone, E.
AU - Cinti, R.
AU - Ravazzolo, R.
AU - Scartezzini, P.
PY - 2001
Y1 - 2001
N2 - 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 served 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.
AB - 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 served 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.
UR - http://www.scopus.com/inward/record.url?scp=0034811308&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034811308&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2001.5169
DO - 10.1006/bbrc.2001.5169
M3 - Article
C2 - 11444877
AN - SCOPUS:0034811308
VL - 285
SP - 540
EP - 545
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -