Evidence of a yeast proteinase specific for elongation factor 2
| Autor: | Luigi Servillo, Alfonso Giovane, Lucio Quagliuolo, Ciro Balestrieri |
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| Přispěvatelé: | Servillo, Luigi, Quagliuolo, Lucio, Balestrieri, C, Giovane, Alfonso |
| Jazyk: | angličtina |
| Předmět: |
Proteolysis
Biophysics Proteinase Biochemistry Saccharomyces Peptide Elongation Factor 2 Structural Biology Genetics medicine Molecular Biology Gel electrophoresis chemistry.chemical_classification Adenosine Diphosphate Ribose biology medicine.diagnostic_test Proteolytic enzymes Cell Biology NAD Peptide Elongation Factors biology.organism_classification Yeast Elongation factor Enzyme chemistry Peptide Hydrolases |
| Zdroj: | FEBS Letters. (1-2):257-260 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(88)81072-X |
| Popis: | Two proteinases active on elongation factor 2 have been found in yeast. The former hydrolyzes the factor producing a single ADP-ribosylatable fragment, whereas it does not produce any fragment when incubated with different proteins. The latter, less specific, is active in cleaving both EF-2 and other proteins giving rise to a noticeable number of fragments. Moreover, when native EF-2 is incubated with the most specific of the two proteinases, the amount of the ADP-ribosylatable fragment increases with time, while no fragments are evident when ADP-ribosylation of EF-2 comes before its incubation with the proteolytic enzyme. A possible regulatory role of this proteinase on EF-2 turnover is hypothesized. |
| Databáze: | OpenAIRE |
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