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Literature summary for 4.6.1.23 extracted from

  • Alford, S.; Pearson, J.; Carette, A.; Ingham, R.; Howard, P.
    alpha-Sarcin catalytic activity is not required for cytotoxicity (2009), BMC Biochem., 10, 9-9.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.23

Cloned(Commentary)

Cloned (Comment) Organism
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 Aspergillus giganteus

Protein Variants

Protein Variants Comment Organism
H137Q similar to the wild-type and mutant R121Q, this mutant is cytotoxic in HeLa cells or Cos-7 cells in a dose-dependent manner. Both GFP and luciferase expression are not inhibited Aspergillus giganteus
R121Q despite its reduced catalytic ability in vitro, the mutant is cytotoxic in HeLa cells or Cos-7 cells in a dose-dependent manner, that is only slightly reduced from that observed for wild-type. Both GFP and luciferase expression are not inhibited Aspergillus giganteus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm both mutant and wild-type variants of alpha-sarcin localize to the nucleus and cytoplasm, where they colocalize with ribosomal marker RPS6 Aspergillus giganteus 5737
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nucleus both mutant and wild-type variants of alpha-sarcin localize to the nucleus and cytoplasm, where they colocalize with ribosomal marker RPS6 Aspergillus giganteus 5634
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Organism

Organism UniProt Comment Textmining
Aspergillus giganteus
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-
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Synonyms

Synonyms Comment Organism
alpha-sarcin
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 Aspergillus giganteus

General Information

General Information Comment Organism
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 Aspergillus giganteus
physiological function both alpha-sarcin and ricin transfected cells demonstrate a dose-dependent decrease in viability at 48 hours, whereby ricin is more effective at low doses (50 ng) than alpha-sarcin. At concentrations greater than 250 ng, no further reduction in viability and approximately 20% of the cells remain viable. Direct cytoplasmic expression of alpha-sarcin and ricin in mammalian cells is cytotoxic: exogenous expression of both alpha-sarcin and ricin in HeLa cells results in decreased viability within 48 hours. Both alpha-sarcin and ricin induce cell death at similar rates, with ricin exhibiting slightly enhanced cytotoxicity. Direct expression of alpha-sarcin in Cos-7 cells also results in cytotoxicity. Although protein synthesis inhibition likely contributes to cell death, it is not required. alpha-Sarcin can promote cell death through a mechanism that is independent of rRNA cleavage and Jun N-terminal kinase activation Aspergillus giganteus