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Information on EC 4.6.1.23 - ribotoxin and Organism(s) Aspergillus giganteus and UniProt Accession P00655

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EC Tree
     4 Lyases
         4.6 Phosphorus-oxygen lyases
             4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
                4.6.1.23 ribotoxin
IUBMB Comments
Ribotoxins are rRNA endonucleases that catalyse the cleavage of the phosphodiester bond between guanosine and adenosine residues at one specific position in 28S rRNA. The enzyme secreted by Aspergillus giganteus specifically cleaves rat 28S rRNA between G4325 and A4326 and displays cytotoxic activity toward animal cells. It can also act on bacterial rRNAs. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
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Aspergillus giganteus
UNIPROT: P00655
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The taxonomic range for the selected organisms is: Aspergillus giganteus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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a 28S rRNA containing guanosine-adenosine pair
+
H2O
=
an [RNA fragment]-3'-adenosine-3'-phosphate
+
a 5'-hydroxy-guanosine-3'-[RNA fragment]
a 28S rRNA containing guanosine-adenosine pair
+
=
an [RNA fragment]-3'-adenosine-3'-phosphate
+
a 5'-hydroxy-guanosine-3'-[RNA fragment]
Synonyms
alpha-sarcin, restrictocin, ribotoxin, mitogillin, ageritin, ribonuclease alpha-sarcin, rrna endonuclease, alpha-sarcin-like ribotoxin restrictocin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonuclease alpha-sarcin
-
alpha-sarcin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
-
-
endoribonuclease reaction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[28S-rRNA]-guanosine-adenosine 5'-hydroxy-guanosine-ribonucleotide-3'-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3'-adenosine-2',3'-cyclophosphate-forming and hydrolysing)
Ribotoxins are rRNA endonucleases that catalyse the cleavage of the phosphodiester bond between guanosine and adenosine residues at one specific position in 28S rRNA. The enzyme secreted by Aspergillus giganteus specifically cleaves rat 28S rRNA between G4325 and A4326 and displays cytotoxic activity toward animal cells. It can also act on bacterial rRNAs. The enzyme catalyses a two-stage endonucleolytic cleavage. The first reaction produces 5'-hydroxy-phosphooligonucletides and 3'-phosphooligonucleotides ending with 2',3'-cyclic phosphodiester, which are released from the enzyme. The enzyme then hydrolyses these cyclic compounds in a second reaction that takes place only when all the susceptible 3',5'-phosphodiester bonds have been cyclised. The second reaction is a reversal of the first reaction using the hydroxyl group of water instead of the 5'-hydroxyl group of ribose. The overall process is that of a phosphorus-oxygen lyase followed by hydrolysis to form the 3'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY hide
1407-48-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
show the reaction diagram
-
-
-
?
ApA + H2O
3'-AMP + adenosine
show the reaction diagram
-
-
-
?
CpC + H2O
?
show the reaction diagram
-
-
-
?
Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
show the reaction diagram
-
-
-
?
poly(A) + H2O
?
show the reaction diagram
-
-
-
?
ribosomes + H2O
?
show the reaction diagram
-
-
-
?
RNA + H2O
?
show the reaction diagram
hydrolyzes naked RNA at purines in both single-and double-stranded regions
-
-
?
rRNA + H2O
?
show the reaction diagram
-
-
-
?
sarcin/ricin ribosomal loop RNA + H2O
?
show the reaction diagram
-
-
-
?
23S rRNA + H2O
?
show the reaction diagram
-
cleavage of sarcin-ricin loop of 23S rRNA inhibits in vitro translation, slightly affects binding of elongation factor Tu ternary complex to the ribosome, inhibits elongation factor G binding, and consequently GTP hydrolysis and mRNA-tRNA translocation
-
-
?
28 S rRNA + H2O
alpha-fragment from the 3' end of 28S rRNA
show the reaction diagram
70S ribosomes + H2O
?
show the reaction diagram
-
-
-
-
?
ApA + H2O
3'-AMP + adenosine
show the reaction diagram
Escherichia coli 23S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
show the reaction diagram
-
-
-
-
?
Escherichia coli 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
show the reaction diagram
-
-
-
-
?
GpA + H2O
3'-GMP
show the reaction diagram
-
hydrolysis of the 3'-5' phosphodiester bond of the substrate yields 2',3'-cyclic adenosine mononucleotide, this intermediate is converted into the corresponding 3'-monophosphate derivative as the final product of the reaction
-
-
?
Rattus norvegicus 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
show the reaction diagram
-
alpha-sarcin hydrolyzes a phosphodiester bond on the 3' side of a guanine residue 393 nucleotides from the 3' end. The alpha-sarcin domain is composed of a purine-rich sequence of 14 highly conserved nucleotides
-
-
?
RNA + H2O
?
show the reaction diagram
Saccharomyces cerevisiae 28S rRNA containing guanosine-adenosine pair + H2O
an [RNA fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-[RNA fragment]
show the reaction diagram
-
-
-
-
?
supercoiled double-stranded DNA + H2O
nicked circular conformation of DNA
show the reaction diagram
yeast 25S RNA + H2O
?
show the reaction diagram
-
-
-
-
?
yeast 26 S RNA + H2O
?
show the reaction diagram
-
alpha-sarcin cleaves the phosphodiester bond between the guanine residue at position 3025 and the adenine residue at position 3026
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
rRNA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
-
the ribosome-inactivating proteins alpha-sarcin targets the ribosomal sarcin/ricin loop, specific recognition and cleavage. The eukaryotic ribosomal stalk directly interacts with several members of the N-glycosidase family, favoring their disruption of the sarcin/ricin loop, overview. alpha-Sarcin does not interact with the P1/P2 C-terminal peptide SDDDMGFGLFD
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
elongation factor G
the transitory binding of elongation factor G and GDP to the ribosome inhibits the rate of alpha-sarcin cleavage. The stabilization of this binding with fusidic acid completely prevents alpha-sarcin cleavage
-
GDP
the transitory binding of elongation factor G and GDP to the ribosome inhibits the rate of alpha-sarcin cleavage. The stabilization of this binding with fusidic acid completely prevents alpha-sarcin cleavage
Thiostrepton
irreversible binding of the antibiotic thiostrepton to the Escherichia coll ribosome decreases the rate of cleavage by alpha-sarcin approximately 2fold
Cibacron blue F3GA
-
-
Mg2+
-
inhibits hydrolysis of RNA
Sodium dodecyl sulfate
-
reversible inhibition of ribonuclease activity, irreversible inhibition of deoxyribonuclease activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ribosomal stalk
-
the eukaryotic ribosomal stalk directly interacts with several members of the N-glycosidase family, favoring their disruption of the SRL
-
additional information
-
P1 protein isozymes P1alphaP2beta and P1betaP2alpha are acidic proteins that are extremely dynamic, including their exchange with the cytoplasmic pool, their C-terminal regions being responsible for the interaction, recruitment, and regulation of supernatant translation factors and ribosome-inactivating proteins like ricin and trichosanthin, but alpha-sarcin does not interact with the P1/P2 C-terminal peptide SDDDMGFGLFD
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.043
ApA
0.027 - 0.045
ApA
0.0036
GpA
-
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 0.0001
ApA
0.917
28 S rRNA
-
0.000012 - 0.00027
ApA
0.000009
GpA
-
pH 7.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
specific activity 18200 units/mg, 1 unit is the amount of protein causing 50% inhibition of protein synthesis in 0.001 ml of rabbit-reticulocyte lysate system
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 8.5
-
no activity below pH 2.5 or above pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
18500 Dalton pro-protein
-
Manually annotated by BRENDA team
22500 Dalton pre-pro-protein
-
Manually annotated by BRENDA team
alpha-sarcin proteins are exclusively localized in large and small vacuoles
Manually annotated by BRENDA team
-
both mutant and wild-type variants of alpha-sarcin localize to the nucleus and cytoplasm, where they colocalize with ribosomal marker RPS6
Manually annotated by BRENDA team
-
both mutant and wild-type variants of alpha-sarcin localize to the nucleus and cytoplasm, where they colocalize with ribosomal marker RPS6
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutations in alpha-sarcin, which impair alpha-sarcin's ability to inhibit protein synthesis, do not affect its cytotoxicity. The mutants are unable to activate Jun N-terminal kinase, thus the sarcin-ricin loop remains intact indicating that the alpha-sarcin mutants are catalytically inactive
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNAS_ASPGI
177
0
19724
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
x * 45000, recombinant His-tagged enzyme fusion construct scFvA33alphasarcin, SDS-PAGE
additional information
-
15N-1H residual dipolar coupling NMR, alkyl poly(ethylene glycol)/alcohol mixture, 1 mM, pH 6.0, 25°C
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45000, recombinant His-tagged enzyme fusion construct scFvA33alphasarcin, SDS-PAGE
dimer
-
dimeric form fails to inactivate ribosomes as well as to hydrolyze mini-stem-loop RNA, but is an effective ribonuclease in situ
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
alpha-sarcin is synthesized in an inactive precursor form and segregated and matured in the membrane compartment
ribonucleoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure
15N-1H residual dipolar coupling NMR, alkyl poly(ethylene glycol)/alcohol mixture, 1 mM, pH 6.0, 25°C, 24 Hz
-
alpha-sarcin three-dimensional structure determined by X-ray diffraction of single crystals of the toxin
-
circular dichroism studies. The protein contains about 40% of periodic structures, mainly located at both extremes of the polypeptide chain. beta-Turns and aperiodic conformation appear at the central part of the molecule
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N54A
mutation in a conserved residue located in loop 2 of the protein, decrease in melting temperature. About 65% of wild-type activity with ribosomes and ribosomal loop RNA
N54D
mutation in a conserved residue located in loop 2 of the protein, decrease in melting temperature. About 60% of wild-type activity with ribosomes and ribosomal loop RNA
N54Q
mutation in a conserved residue located in loop 2 of the protein, decrease in melting temperature. About 24% and 68% of wild-type activity with ribosomes and ribosomal loop RNA, respectively
N54S
mutation in a conserved residue located in loop 2 of the protein, decrease in melting temperature. About 28 and 49% of wild-type activity with ribosomes and ribosomal loop RNA, respectively
N54Y
mutation in a conserved residue located in loop 2 of the protein, decrease in melting temperature. Loss of activity
Y48F
mutant is produced in Escherichia coli and purified to homogeneity (ca. 3 mg/l of original bacterial culture)
C148S
-
point mutation constructed from cDNA clone
C6S
-
point mutation constructed from cDNA clone
E125I
-
site-directed mutagenesis
E96A
-
mutagenised using the T7-GEN TM in vitro mutagenesis kit, 80% less cytotoxity to HeLa cells
E96Q
-
mutagenesis variant protein
H137Q
H50/137Q
-
mutagenesis variant protein
H50/137Q/E96Q
-
mutagenesis variant protein
H50Q
-
mutagenesis variant protein
H50Q/H137Q/E96Q
-
catalytically inactive alpha-sarcin mutant sar3M
I129C
-
site-directed mutagenesis
L145F
-
oligonucleotide-site directed mutagenesis, retains cytotoxic activity
R121K
-
oligonucleotide site-directed mutagenesis
R121Q
additional information
-
method development for engineering of alpha-sarcin splicing, overview. The splicing constructs, NSar-VMAN-FKBP and FRB-VMAC-CSar splice poorly, and the intein-alpha-sarcin splice junctions interfere with splicing
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8.5
additional information
-
five different pH-induced conformational transitions are detected. Two of them, at pH 2.5 and 10.2, are denaturing transitions
752836
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
melting temperature, mutants N54D, N54A
45
melting temperature, mutants N54Q
46
melting temperature, mutants N54S, N54Y
52
melting temperature of wild-type
54
-
L145F mutant variant, increased transition temperature Tm
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
deletion mutant DELTA(7-22)
L145F mutant variant
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
deletion mutant delta(7-22) produced in Escherichia coli
expression in Escherichia coli
expression in wheat germ cell-free system
alpha-sarcin cDNA cloned by consecutive annealing of overlapping primers followed by ligation into XhoI- and HindIII-sites in pcDNA3.1 or pcDNA3-mychis vector (C-terminal MycHis tag). alpha-Sarcin cDNA cloned into 3 × FLAG pMSCV to obtain a N-terminal 3 × Flag tagged version of alpha-sarcin. Expression of wild-type and mutant constructs in HeLa or Cos-7 cells
-
cloned and expressed in Escherichia coli
-
cloned and expressed in Escherichia coli BL21(DE3)
-
cloned and expressed in Escherichia coli RB791
-
cloned and expressed in Escherichia coli TG2
-
cloning of the genomic alpha-sarcin gene pGEM-T/FL-alpha plasmid, construction of the alpha-sarcin gene and its mutants by PCR, using genomic DNA as template
-
doxycycline-inducible intracellular expression of wild-type alpha-sarcin in Saccharomyces cerevisiae strain W303 and in strains deficient for P1 or P2 protein, wild-type alpha-sarcin is lethal in all wild-type yeast clones, while 30% and 80% of resistant clones are obtained for the DELTAP1alphaP2beta and DELTAP2 strains, respectively
-
recombinant expression of FLAG3-tagged alpha-sarcin in HeLa cells, alpha-sarcin splicing is incduced by and dependent on rapamycin, is inducible with rapid kinetics, and triggers apoptosis in the cytoplasm of HeLa cells
-
recombinant extracellular His-tagged enzyme fusion construct scFvA33alphasarcin from expression in Pichia pastoris strain KM71 by nickel affinity chromatgraphy
-
the His-tagged enzyme is fused to the single-chain variable fragment (scFv) of the monoclonal antibody that targets GPA33, the construct scFvA33alphasarcin is expressed in Pichia pastoris strain KM71 using the AOX1 promoter, subcloning in Escherichia coli DH5aF cells, and secretion to the medium
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Endo, Y.; Wool, I.G.
The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28 S ribosomal ribonucleic acid
J. Biol. Chem.
257
9054-9060
1982
Aspergillus giganteus
Manually annotated by BRENDA team
Endo, Y.; Huber, P.W.; Wool, I.G.
The ribonuclease activity of the cytotoxin alpha-sarcin. The characteristics of the enzymatic activity of alpha-sarcin with ribosomes and ribonucleic acids as substrates
J. Biol. Chem.
258
2662-2667
1983
Aspergillus giganteus
Manually annotated by BRENDA team
Wool, I.G.
The mechanism of the action of the cytotoxic nuclease alpha-sarcin and its use to analyze ribosome structure
Trends Biochem. Sci.
9
14-17
1984
Aspergillus giganteus
-
Manually annotated by BRENDA team
Stirpe, F.; Bailey, S.; Miller, S.P.; Bodley, J.W.
Modification of ribosomal RNA by ribosome-inactivating proteins from plants
Nucleic Acids Res.
16
1349-1357
1988
Aspergillus giganteus
Manually annotated by BRENDA team
Ling, J.; Liu, W.; Wang, T.P.
Cleavage of supercoiled double-stranded DNA by several ribosome-inactivating proteins in vitro
FEBS Lett.
345
143-146
1994
Aspergillus giganteus
Manually annotated by BRENDA team
Gasset, M.; Mancheno, J.M.; Laynez, J.; Lacadena, J.; Fernandez-Ballester, G.; Martinez del Pozo, A.; Onaderra, M.; Gavilanes, J.G.
Thermal unfolding of the cytotoxin alpha-sarcin: phospholipid binding induces destabilization of the protein structure
Biochim. Biophys. Acta
1252
126-134
1995
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Lacadena, J.; Mancheno, J.M.; Martinez-Ruiz, A.; Martinez del Pozo, A.; Gasset, M.; Onaderra, M.; Gavilanes, J.G.
Substitution of histidine-137 by glutamine abolishes the catalytic activity of the ribosome-inactivating protein alpha-sarcin
Biochem. J.
309
581-586
1995
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Campos-Olivas, R.; Bruix, M.; Santoro, J.; Martinez del Pozo, A.; Lacadena, J.; Gavilanes, J.G.; Rico, M.
Structural basis for the catalytic mechanism and substrate specificity of the ribonuclease alpha-sarcin
FEBS Lett.
399
163-165
1996
Aspergillus giganteus
Manually annotated by BRENDA team
Cheung, J.I.; Wang, Y.R.; Lin, A.
Substrate specificity of monomeric and dimeric alpha-sarcin
FEBS Lett.
386
60-64
1996
Aspergillus giganteus
Manually annotated by BRENDA team
Sylvester, I.D.; Roberts, L.M.; Lord, J.M.
Characterization of prokaryotic recombinant Aspergillus ribotoxin alpha-sarcin
Biochim. Biophys. Acta
1358
53-60
1997
Aspergillus giganteus
Manually annotated by BRENDA team
Hao, J.J.; Xu, Y-z.; Geng, C.d.; Liu, W.Y.; Wang, E.d; Gong, Z.z.; Ulbrich, N.
Purification of alpha-sarcin and an antifungal protein from Aspergillus giganteus by blue sepharose CL-6B affinity chromatography
Protein Expr. Purif.
14
295-301
1998
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Lacadena, J.; Martinez del Pozo, A.; Lacadena, V.; Martinez-Ruiz, A.; Mancheno, J.M.; Onaderra, M.; Gavilanes, J.G.
The cytotoxin alpha-sarcin behaves as a cyclizing ribonuclease
FEBS Lett.
424
46-48
1998
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Perez-Canadillas, J.M.; Campos-Olivas, R.; Lacadena, J.; Martinez del Pozo, A.; Gavilanes, J.G.; Santoro, J.; Rico, M.; Bruix, M.
Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alpha-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function
Biochemistry
37
15865-15876
1998
Aspergillus giganteus
Manually annotated by BRENDA team
Lacadena, J.; Martinez del Pozo, A.; Martinez-Ruiz, A.; Perez-Canadillas, J.M.; Bruix, M.; Mancheno, J.M.; Onaderra, M.; Gavilanes, J.G.
Role of histidine-50, glutamic acid-96, and histidine-137 in the ribonucleolytic mechanism of the ribotoxin alpha-sarcin
Proteins
37
474-484
1999
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Hwu, L.; Huang, K.; Chen, D.; Lin, A.
The action mode of the ribosome-inactivating protein alpha-sarcin
J. Biomed. Sci.
7
420-428
2000
Aspergillus giganteus
Manually annotated by BRENDA team
Perez-Canadillas, J.M.; Santoro, J.; Campos-Olivas, R.; Lacadena, J.; Martinez del Pozo, A.; Gavilanes, J.G.; Rico, M.; Bruix, M.
The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity
J. Mol. Biol.
299
1061-1073
2000
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Xu, Y.Z.; Liu, W.Y.
Effects of the active aldehyde group generated by RNA N-glycosidase in the sarcin/ricin domain of rat 28S ribosomal RNA on peptide elongation
Biol. Chem.
381
113-119
2000
Aspergillus giganteus
Manually annotated by BRENDA team
Masip, M.; Lacadena, J.; Mancheno, J.M.; Onaderra, M.; Martinez-Ruiz, A.; Martinez del Pozo, A.; Gavilanes, J.G.
Arginine 121 is a crucial residue for the specific cytotoxic activity of the ribotoxin alpha-sarcin
Eur. J. Biochem.
268
6190-6196
2001
Aspergillus giganteus
Manually annotated by BRENDA team
Olmo, N.; Turnay, J.; Gonzalez de Buitrago, G.; Lopez de Silanes, I.; Gavilanes, J.G.; Lizarbe, M.A.
Cytotoxic mechanism of the ribotoxin alpha-sarcin. Induction of cell death via apoptosis
Eur. J. Biochem.
268
2113-2123
2001
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Garcia-Ortega, L.; Masip, M.; Mancheno, J.M.; Onaderra, M.; Lizarbe, M.A.; Garcia-Mayoral, M.F.; Bruix, M.; Martinez del Pozo, A.; Gavilanes, J.G.
Deletion of the NH2-terminal beta-hairpin of the ribotoxin alpha-sarcin produces a nontoxic but active ribonuclease
J. Biol. Chem.
277
18632-18639
2002
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Larsson, S.L.; Sloma, M.S.; Nygard, O.
Conformational changes in the structure of domains II and V of 28S rRNA in ribosomes treated with the translational inhibitors ricin or alpha-sarcin
Biochim. Biophys. Acta
1577
53-62
2002
Aspergillus giganteus
Manually annotated by BRENDA team
Liu, R.s.; Huang, H.; Yang, Q.; Liu, W.Y.
Purification of alpha-sarcin and an antifungal protein from mold (Aspergillus giganteus) by chitin affinity chromatography
Protein Expr. Purif.
25
50-58
2002
Aspergillus giganteus, Aspergillus giganteus MDH 18894
Manually annotated by BRENDA team
Masip, M.; Garcia-Ortega, L.; Olmo, N.; Garcia-Mayoral, M.F.; Perez-Canadillas, J.M.; Bruix, M.; Onaderra, M.; Martinez del Pozo, A.; Gavilanes, J.G.
Leucine 145 of the ribotoxin alpha-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein
Protein Sci.
12
161-169
2003
Aspergillus giganteus
Manually annotated by BRENDA team
Perez-Canadilllas, J.M.; Garcia-Mayoral, M.F.; Laurents, D.V.; Martinez del Pozo, A.; Gavilanes, J.G.; Rico, M.; Bruix, M.
Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases
FEBS Lett.
534
197-201
2003
Aspergillus giganteus
Manually annotated by BRENDA team
Garcia-Mayoral, M.F.; Pantoja-Uceda, D.; Santoro, J.; Martinez del Pozo, A.; Gavilanes, J.G.; Rico, M.; Bruix, M.
Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings
Eur. Biophys. J.
34
1057-1065
2005
Aspergillus giganteus
Manually annotated by BRENDA team
Alvarez-Garcia, E.; Garcia-Ortega, L.; Verdun, Y.; Bruix, M.; Martinez del Pozo, A.; Gavilanes, J.G.
Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of alpha-sarcin
Biol. Chem.
387
535-541
2006
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Herrero-Galan, E.; Lacadena, J.; Martinez Del Pozo, A.; Boucias, D.G.; Olmo, N.; Onaderra, M.; Gavilanes, J.G.
The insecticidal protein hirsutellin A from the mite fungal pathogen Hirsutella thompsonii is a ribotoxin
Proteins
72
217 - 228
2008
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Alford, S.; Pearson, J.; Carette, A.; Ingham, R.; Howard, P.
alpha-Sarcin catalytic activity is not required for cytotoxicity
BMC Biochem.
10
9-9
2009
Aspergillus giganteus
Manually annotated by BRENDA team
Garcia-Ortega, L.; Alvarez-Garcia, E.; Gavilanes, J.G.; Martinez-Del-Pozo, A.; Joseph, S.
Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding
Nucleic Acids Res.
38
4108-4119
2010
Aspergillus giganteus
Manually annotated by BRENDA team
Alford, S.C.; OSullivan, C.; Obst, J.; Christie, J.; Howard, P.L.
Conditional protein splicing of alpha-sarcin in live cells
Mol. Biosyst.
10
831-837
2014
Aspergillus giganteus
Manually annotated by BRENDA team
Carreras-Sangra, N.; Tome-Amat, J.; Garcia-Ortega, L.; Batt, C.A.; Onaderra, M.; Martinez-del-Pozo, A.; Gavilanes, J.G.; Lacadena, J.
Production and characterization of a colon cancer-specific immunotoxin based on the fungal ribotoxin alpha-sarcin
Protein Eng. Des. Sel.
25
425-435
2012
Aspergillus giganteus, Aspergillus giganteus MDH18894
Manually annotated by BRENDA team
He, K.; Zhou, H.R.; Pestka, J.J.
Mechanisms for ribotoxin-induced ribosomal RNA cleavage
Toxicol. Appl. Pharmacol.
265
10-18
2012
Aspergillus giganteus
Manually annotated by BRENDA team
Miller, S.P.; Bodley, J.W.
Alpha-sarcin cleaves ribosomal RNA at the alpha-sarcin site in the absence of ribosomal proteins
Biochem. Biophys. Res. Commun.
154
404-410
1988
Aspergillus giganteus, Aspergillus giganteus MH18894
Manually annotated by BRENDA team
Martinez del Pozo, A.; Gasset, M.; Onaderra, M.; Gavilanes, J.G.
Conformational study of the antitumor protein alpha-sarcin
Biochim. Biophys. Acta
953
280-288
1988
Aspergillus giganteus
Manually annotated by BRENDA team
Siemer, A.; Masip, M.; Carreras, N.; Garcia-Ortega, L.; Onaderra, M.; Bruix, M.; Del Pozo, A.M.; Gavilanes, J.G.
Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity
Biol. Chem.
385
1165-1170
2004
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Wawrzynczak, E.J.; Henry, R.V.; Cumber, A.J.; Parnell, G.D.; Derbyshire, E.J.; Ulbrich, N.
Biochemical, cytotoxic and pharmacokinetic properties of an immunotoxin composed of a mouse monoclonal antibody Fib75 and the ribosome-inactivating protein alpha-sarcin from Aspergillus giganteus
Eur. J. Biochem.
196
203-209
1991
Aspergillus giganteus (P00655), Aspergillus giganteus
Manually annotated by BRENDA team
Marchant, A.; Hartley, M.R.
Mutational studies on the alpha-sarcin loop of Escherichia coli 23S ribosomal RNA
Eur. J. Biochem.
226
141-147
1994
Aspergillus giganteus
Manually annotated by BRENDA team
Chan, Y.L.; Endo, Y.; Wool, I.G.
The sequence of the nucleotides at the alpha-sarcin cleavage site in rat 28 S ribosomal ribonucleic acid
J. Biol. Chem.
258
12768-12770
1983
Aspergillus giganteus
Manually annotated by BRENDA team
Miller, S.P.; Bodley, J.W.
Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome
Nucleic Acids Res.
19
1657-1660
1991
Aspergillus giganteus (P00655)
Manually annotated by BRENDA team
Endo, Y.; Oka, T.; Tsurugi, K.; Natori, Y.
The biosynthesis of a cytotoxic protein, alpha-sarcin, in a mold Aspergillus giganteus. I. Synthesis of prepro- and pro-alpha-sarcin in vitro
Tokushima J. Exp. Med.
40
1-6
1993
Aspergillus giganteus (P00655), Aspergillus giganteus
Manually annotated by BRENDA team
Endo, Y.; Oka, T.; Yokota, S.; Tsurugi, K.; Natori, Y.
The biosynthesis of a cytotoxic protein, alpha-sarcin, in a mold of Aspergillus giganteus. II. Maturation of precursor form of alpha-sarcin in vivo
Tokushima J. Exp. Med.
40
7-12
1993
Aspergillus giganteus (P00655), Aspergillus giganteus
Manually annotated by BRENDA team