[Effect of the topography of the signal peptidase site on the effectiveness of secretion of recombinant human granulocyte-macrophage colony-stimulating factor into Escherichia coli periplasm]

Autor: L E, Petrovskaia, E A, Kriukov, S A, Iakimov, A N, Vul'fson, R A, Alibaeva, L N, Shingarova, A A, Guzaev, V M, Abramov, V G, Korobko
Rok vydání: 1995
Předmět:
Zdroj: Bioorganicheskaia khimiia. 21(12)
ISSN: 0132-3423
Popis: Synthesis of an artificial gene encoding the signal peptide of the Yersinia pestis capsule antigen (Caf1) was accomplished. A set of plasmids coding for hybrid proteins in which a modified sequence of the Caf1 signal peptide is connected to the amino acid sequence of the mature granulocyte-macrophage colony stimulating factor (GM-CSF) were constructed. Topography of the cleavage site of signal proteases was studied. The presence of an arginine residue within the N-terminal part of the mature human GM-CSF was shown to hinder the proper processing and translocation of the precursor through periplasmic membrane. A number of E. coli strains secreting biologically active mutants of human GM-CSF were obtained.
Databáze: OpenAIRE