| Autor: |
Olombrada M; Departamento de Bioquímica y Biología Molecular I, Facultad de Química, Universidad Complutense , 28040 Madrid, Spain., Rodríguez-Mateos M, Prieto D, Pla J, Remacha M, Martínez-del-Pozo A, Gavilanes JG, Ballesta JP, García-Ortega L |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 2014 Mar 18; Vol. 53 (10), pp. 1545-7. Date of Electronic Publication: 2014 Mar 04. |
| DOI: |
10.1021/bi401470u |
| Abstrakt: |
The ribosomal sarcin/ricin loop (SRL) is the target of ribosome-inactivating proteins like the N-glycosidase ricin and the fungal ribotoxin α-sarcin. The eukaryotic ribosomal stalk directly interacts with several members of the N-glycosidase family, favoring their disruption of the SRL. Here we tested this hypothesis for the ribotoxin α-sarcin. Experiments with isolated ribosomes, cell-free translation systems, and viability assays with Saccharomyces cerevisiae strains defective in acidic stalk proteins showed that the inactivation exerted by α-sarcin is independent of the composition of the ribosomal stalk. Therefore, α-sarcin, with the same ribosomal target as ricin, seems to access the SRL by a different pathway. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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