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  • Title: The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing.
    Author: Germain D, Dumas F, Vernet T, Bourbonnais Y, Thomas DY, Boileau G.
    Journal: FEBS Lett; 1992 Mar 16; 299(3):283-6. PubMed ID: 1544507.
    Abstract:
    We have produced in the baculovirus/insect cells expression system a soluble secreted form of the Saccharomyces cerevisiae Kex2 endoprotease. This secreted enzyme was purified and its NH2-terminal sequence determined. The NH2-terminal sequence started at residue Leu109 of the sequence deduced from the KEX2 gene nucleotide sequence, showing that the Kex2 enzyme is produced as a proenzyme. Residue Leu109 is preceded by a pair of basic amino acid residues (Lys107-Arg108) which is a potential processing site for the Kex2 endopeptidase. Furthermore, expression of an inactive form of this truncated enzyme resulted in the production of a protein with a higher molecular weight. These observations suggest that the pro-region of Kex2 endoprotease is removed by a self-processing event.
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