The pro‐region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self‐processing
- 1 March 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 299 (3) , 283-286
- https://doi.org/10.1016/0014-5793(92)80132-z
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.Keywords
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