Processed enzymatically active protease (p15gag) of avian retrovirus obtained in an E. coli system expressing a recombinant precursor (Pr25lac-delta gag)
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články
PubMed
2844587
DOI
10.1016/0014-5793(88)80198-4
PII: 0014-5793(88)80198-4
Knihovny.cz E-zdroje
- MeSH
- antigeny virové genetika MeSH
- Escherichia coli genetika MeSH
- genové produkty gag MeSH
- geny * MeSH
- molekulární sekvence - údaje MeSH
- rekombinantní proteiny biosyntéza MeSH
- Retroviridae - proteiny genetika MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- virové geny * MeSH
- virus ptačí leukózy genetika MeSH
- virus ptačí myeloblastózy enzymologie genetika MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- antigeny virové MeSH
- genové produkty gag MeSH
- rekombinantní proteiny MeSH
- Retroviridae - proteiny MeSH
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 p15gag is cut off the carboxy-terminus of a gag polyprotein precursor, Pr76gag. We report here that direct and efficient production of the avian retrovirus processing protease p15gag (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 (Pr25lac-delta gag) was accompanied by its structurally accurate processing.
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