Vaccinia virus encodes a protein with similarity to glutaredoxins

Johnson, Gerard P.; Goebel, Scott J.; Perkus, Marion E.; Davis, Stephen W.; Winslow, Joseph P.; Paoletti, Enzo

doi:10.1016/0042-6822(91)90508-9

Cited by 35 publications

(15 citation statements)

References 47 publications

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“…The thiotransferase/ glutaredoxin active site (15) found in ADNP (Fig. 1) may modulate its own DNA binding activity or that of other DNAbinding proteins in response to oxidative stress and signal transduction pathways implicated in the redox state of the cell (27).…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of the Human Activity-dependent Neuroprotective Protein

Zamostiano¹,

Pinhasov²,

Gelber³

et al. 2001

Journal of Biological Chemistry

220

250

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We have recently cloned the mouse activity-dependent neuroprotective protein (ADNP). Here, we disclose the cloning of human ADNP (hADNP) from a fetal brain cDNA library. Comparative sequence analysis of these two ADNP orthologs indicated 90% identity at the mRNA level. Several single nucleotide polymorphic sites were noticed. The deduced protein structure contained nine zinc fingers, a proline-rich region, a nuclear bipartite localization signal, and a homeobox domain profile, suggesting a transcription factor function. Further comparative analysis identified an ADNP paralog (33% identity and 46% similarity), indicating that these genes belong to a novel protein family with a nine-zinc finger motif followed by a homeobox domain. The hADNP gene structure spans ϳ40 kilobases and includes five exons and four introns with alternative splicing of an untranslated second exon. The hADNP gene was mapped to chromosome 20q12-13.2, a region associated with aggressive tumor growth, frequently amplified in many neoplasias, including breast, bladder, ovarian, pancreatic, and colon cancers. hADNP mRNA is abundantly expressed in distinct normal tissues, and high expression levels were encountered in malignant cells. Down-regulation of ADNP by antisense oligodeoxynucleotides up-regulated the tumor suppressor p53 and reduced the viability of intestinal cancer cells by 90%. Thus, ADNP is implicated in maintaining cell survival, perhaps through modulation of p53.Mouse activity-dependent neuroprotective protein (mADNP), 1 a novel vasoactive intestinal peptide (VIP)-responsive gene, was recently cloned (1). The relative enrichment of mADNP transcripts in the cerebellum, cortex, hippocampus, medulla, and midbrain and the increases found in the presence of VIP, an established neuroprotective substance (2), implied a potential function in brain metabolism. Specifically, mADNP mRNA increased 2-3-fold in astroglial cells incubated for 3 h in the presence of nanomolar amounts of VIP (1). Another tissue containing increased mADNP transcripts is the mouse testis, a highly proliferative tissue, suggesting the involvement of ADNP in cell division.As deregulation of oncogenes has been associated with neurodegeneration (3), pathways that regulate neuronal survival may impinge upon cancer proliferation. VIP regulates both neuronal survival and cell division (2). A system whereby labeled VIP is suggested as a tumor marker has been proposed, localizing in vivo tumors of patients with gastrointestinal neuroendocrine cancers as well as pancreatic and colonic adenocarcinomas (4). Other studies have identified a very high incidence of VIP receptor binding in breast, ovarian, endometrial, prostate, bladder, lung, esophageal, colonic, and pancreatic tumors as well as in neuroendocrine and brain tumors (5). However, the VIP effect on cancer growth depends on the specific tumor and may be stimulatory (6, 7) or inhibitory (8). In view of the high incidence of tumors containing VIP receptors, a potential intervention in tumor growth may employ a gene downstr...

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Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of the Human Activity-dependent Neuroprotective Protein

Zamostiano¹,

Pinhasov²,

Gelber³

et al. 2001

Journal of Biological Chemistry

220

250

View full text Add to dashboard Cite

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“…5. The sequences of glutaredoxins from yeast (Gan et al, 1990) and vaccinia virus (Johnson et al, 1991;Ahn and Moss, 1992) are also aligned using the structure of E. coli glutaredoxin to optimize structural similarity. Analysis of the structures was based on the assumption that the basic folding patterns of all glutaredoxins are the same.…”

Section: A C a C T I T G A A A A C T T A A G A C C~~a T G A A G~c T Gmentioning

confidence: 99%

Purification from Placenta, Amino Acid Sequence, Structure Comparisons and cDNA Cloning of Human Glutaredoxin

Padilla

Martı́nez-Galisteo

Bárcena

et al. 1995

European Journal of Biochemistry

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Glutaredoxin is generally a glutathione-dependent hydrogen donor for ribonucleotide reductase and also catalyses general glutathione (GSH)-disulfide-oxidoreduction reactions in the presence of NADPH and glutathione reductase. A Glutaredoxin from human placenta was purified to homogeneity, as judged by SDSPAGE and IEF (12 m a ) . Purification was monitored by the activity with hydroxyethyl disulfide as a substrate. Values of pJ for glutaredoxin were obtained by IEF; the pI of the protein shifted from 7.3 in its fully reduced state to 9.0 in the oxidized state after treatment with excess hydroxyethyl disulfide. The glutaredoxin preparation showed GSH-dependent hydrogen-donor activity with recombinant mouse ribonucleotide reductase, it exhibited dehydroascorbate reductase activity as well as hydroxyethyl-disulfide-reducing activity. The amino acid sequence (residues 3 -104) of glutaredoxin was determined by peptide sequencing and residues 1, 2 and 105 by cDNA sequence analysis. The glutaredoxin sequence comprised the classical active site for glutaredoxins -Cys22-Pro-Tyr-Cys25-and three additional halfcystine residues; two of these in positions 78 and 82. The sequence was similar to other known mammalian glutaredoxins (about 80 % identities), with important differences such as one additional Cys residue (Cys7) and no Met residue. The sequence of human glutaredoxin was compared to that of Escherichia coli glutaredoxin with known three-dimensional structure in solution to indentify conserved residues and predict a structure from alignment. In particular the GSH-binding site of glutaredoxin was conserved between all molecules. A cDNA that encodes the entire glutaredoxin gene (grx) and flanking sequences was isolated from a human spleen cDNA library. The nucleotide sequence of this cDNA (0.8 kb) was determined, including the complete grx gene.

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“…The RASC8 cDNA clone contained a 568 bp insert excluding the synthetic EcoRI and XbaI adaptors and [12], E. coli [2]. '.'…”

Section: Dna Sequence Analysis Of Rasc8mentioning

confidence: 99%

Cloning and sequence analysis of a cDNA encoding rice glutaredoxin

et al. 1994

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A full-length cDNA clone (RASCS) encoding glutaredoxin (thioltransferase) was isolated from a cDNA library of an aleurone layer prepared from a developing seed of rice (Oryza sativa I,.). RASC8,568bp in length, contained an ATG codon and two possible polyadenylation signals, and encoded 112 amino acid residues. Cys-Pro-Phe-Cys, which is the active site and a highly conserved sequence among thioltransferases, was found in the deduced amino acid sequence. RASCS was introduced into an expression vector pMAL.cZ and the translated product possessed thioltransferase activity.

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Vaccinia virus encodes a protein with similarity to glutaredoxins

Cited by 35 publications

References 47 publications

Cloning and Characterization of the Human Activity-dependent Neuroprotective Protein

Cloning and Characterization of the Human Activity-dependent Neuroprotective Protein

Purification from Placenta, Amino Acid Sequence, Structure Comparisons and cDNA Cloning of Human Glutaredoxin

Cloning and sequence analysis of a cDNA encoding rice glutaredoxin

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