[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: Petrovskaia LE, Kriukov EA, Iakimov SA, Vul'fson AN, Alibaeva RA, Shingarova LN, Guzaev AA, Abramov VM, Korobko VG
Jazyk: ruština
Zdroj: Bioorganicheskaia khimiia [Bioorg Khim] 1995 Dec; Vol. 21 (12), pp. 912-9.
Abstrakt: 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: MEDLINE