R0389
Restrictocin from Aspergillus restrictus
lyophilized powder
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About This Item
Application
Restrictocin from Aspergillus restrictus is used to inhibit protein synthesis. It may be useful as a component of immunotoxins [1]. Product R0389 is provided as a lyophilized powder.
Biochem/physiol Actions
Restrictocin from Aspergillus restrictus is a ribosome-inactivating protein that acts by specifically cleaving rRNA. Approximately 70% of the protein is active restrictocin. Restrictocin shares a high degree of amino acid sequence homology with mitogillin, a ribotoxin that cleaves a single phosphodiester bond of the 29S rRNA of eukaryotic ribosomes [2]. Restrictocin is thought to be activated during the process of secretion [1].
Physical form
Lyophilized from 0.3 mL of 0.5% NaCl
signalword
Danger
Hazard Classifications
Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Anita Goyal et al.
Biochemical and biophysical research communications, 295(4), 812-817 (2002-07-20)
Restrictocin is a 149 amino acid ribonucleolytic toxin produced by the fungus Aspergillus, which specifically cleaves a single phosphodiester bond within 28S rRNA resulting in a potent inhibition of protein synthesis in eukaryotic cells. Restrictocin has 12 prolines out of
B Lamy et al.
Nucleic acids research, 19(5), 1001-1006 (1991-03-11)
We describe the cloning and characterization of the gene coding for the ribotoxin restrictocin, from Aspergillus restrictus (gene res, EMBL accession Number X56176). This toxin is a potent inhibitor of protein synthesis in eucaryotes and is of potential interest as
Anton Glück et al.
Biochimica et biophysica acta, 1594(1), 115-126 (2002-02-05)
A series of contiguous deletions were made in a cDNA encoding the ribonuclease restrictocin with the purpose of identifying the amino acids that are essential for the cleavage of the phosphodiester bond on the 3' side of G4325 in the
Matthew J Plantinga et al.
Biochemistry, 50(14), 3004-3013 (2011-03-23)
Restrictocin and related fungal endoribonucleases from the α-sarcin family site-specifically cleave the sarcin/ricin loop (SRL) on the ribosome to inhibit translation and ultimately trigger cell death. Previous studies showed that the SRL folds into a bulged-G motif and tetraloop, with
X Yang et al.
Nature structural biology, 8(11), 968-973 (2001-10-31)
The cytotoxin sarcin disrupts elongation factor binding and protein synthesis by specifically cleaving one phosphodiester bond in ribosomes. To elucidate the molecular basis of toxin action, we determined three cocrystal structures of the sarcin homolog restrictocin bound to different analogs
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