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Literature summary for 4.6.1.23 extracted from

  • 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 (2010), Nucleic Acids Res., 38, 4108-4119.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.23

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ for ribosome cleavage Aspergillus giganteus

Organism

Organism UniProt Comment Textmining
Aspergillus giganteus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Aspergillus giganteus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
23S rRNA + H2O 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 Aspergillus giganteus ?
-
 ?
70S ribosomes + H2O
-
 Aspergillus giganteus ?
-
 ?

Synonyms

Synonyms Comment Organism
alpha-sarcin
-
 Aspergillus giganteus

General Information

General Information Comment Organism
physiological function alpha-sarcin cleaves the large 23S rRNA at the universally conserved sarcin-ricin loop leading to complete inactivation of the ribosome and cellular death. alpha-Sarcin-treated ribosomes show no defects in mRNA and tRNA binding, peptide-bond formation and sparsomycin-dependent translocation, whereas activity of elongation factor G is strongly impaired Aspergillus giganteus