The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing.
FEBS Lett
; 299(3): 283-6, 1992 Mar 16.
Article
em En
| MEDLINE
| ID: mdl-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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Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Saccharomyces cerevisiae
/
Serina Endopeptidases
/
Subtilisinas
/
Processamento de Proteína Pós-Traducional
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Proteínas de Saccharomyces cerevisiae
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Pró-Proteína Convertases
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article