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The pro‐region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self‐processing
Author(s) -
Germain Doris,
Dumas France,
Vernet Thierry,
Bourbonnais Yves,
Thomas David Y.,
Boileau Guy
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80132-z
Subject(s) - saccharomyces cerevisiae , endopeptidase , biochemistry , enzyme , peptide sequence , chemistry , residue (chemistry) , protein precursor , amino acid residue , amino acid , biology , gene
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 NH 2 ‐terminal sequence determined. The NH 2 ‐terminal sequence started at residue Leu 109 of the sequence deduced from the KEX2 gene nucleotide sequence, showing that the Kex2 enzyme is produced as a proenzyme. Residue Leu 109 is preceded by a pair of basic amino acid residues (Lys 107 ‐Arg 108 ) which is a potential processing site for the Kex2 endopeptidase. Futhermore, 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.