Processed enzymatically active protease (p15 gag) of avian retrovirus obtained in an E. coli system expressing a recombinant precursor (Pr25 lac-Δgag)

Processing proteases of avian and mammalian retroviruses cut the polyprotein precursors encoded by the retroviral genes into mature functional proteins. Retroviral processing proteases are still a rather poorly characterized group as to their relation to other proteases, specificity, and mechanism o...

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Veröffentlicht in:FEBS letters 1988-09, Vol.237 (1), p.187-190
Hauptverfasser: Sedláček, Juraj, Štrop, Petr, Kaprálek, František, Pečenka, Vladimír, Kostka, Vladimír, Trávníček, Miloslav, Říman, Josef
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Sprache:eng
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Zusammenfassung:Processing proteases of avian and mammalian retroviruses cut the polyprotein precursors encoded by the retroviral genes into mature functional proteins. Retroviral processing proteases are still a rather poorly characterized group as to their relation to other proteases, specificity, and mechanism of enzymatic action. In avian retroviruses the generation of the processing protease itself comprises a processing cleavage event — the protease p15 gag is cut off the carboxy-terminus of a gag polyprotein precursor, Pr76 gag . We report here that direct and efficient production of the avian retrovirus processing protease p15 gag (required for structure-function studies and rational design of inhibitors) was obtained in an E. coli system, where massive expression of a size-reduced, recombinant precursor (Pr25 lac-Δgag was accompanied by its structurally accurate processing.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80198-4