Evidence of a yeast proteinase specific for elongation factor 2

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Abstract
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.