The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing
- PMID: 1544507
- DOI: 10.1016/0014-5793(92)80132-z
The pro-region of the Kex2 endoprotease of Saccharomyces cerevisiae is removed by self-processing
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.
Similar articles
-
Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner.FEBS Lett. 1990 Jul 30;268(1):99-102. doi: 10.1016/0014-5793(90)80982-o. FEBS Lett. 1990. PMID: 2116982
-
Expression of the Saccharomyces cerevisiae Kex2p endoprotease in inset cells. Evidence for a carboxy-terminal autoprocessing event.Eur J Biochem. 1992 Feb 15;204(1):121-6. doi: 10.1111/j.1432-1033.1992.tb16613.x. Eur J Biochem. 1992. PMID: 1740121
-
Cleavage of prosomatostatins by the yeast Yap3 and Kex2 endoprotease.Biochimie. 1994;76(3-4):226-33. doi: 10.1016/0300-9084(94)90150-3. Biochimie. 1994. PMID: 7819327
-
Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases.Crit Rev Oncog. 1993;4(2):115-36. Crit Rev Oncog. 1993. PMID: 8420571 Review.
-
Proteolytic processing and regulation.Enzyme. 1991;45(5-6):239-43. doi: 10.1159/000468898. Enzyme. 1991. PMID: 1843278 Review.
Cited by
-
Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site.PLoS One. 2013 Sep 19;8(9):e75347. doi: 10.1371/journal.pone.0075347. eCollection 2013. PLoS One. 2013. PMID: 24069404 Free PMC article.
-
A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease.EMBO J. 1994 May 15;13(10):2280-8. doi: 10.1002/j.1460-2075.1994.tb06510.x. EMBO J. 1994. PMID: 8194519 Free PMC article.
-
Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain ac10: gene cloning and enzyme purification and characterization.Appl Environ Microbiol. 1999 Feb;65(2):611-7. doi: 10.1128/AEM.65.2.611-617.1999. Appl Environ Microbiol. 1999. PMID: 9925590 Free PMC article.
-
Reduced proteolysis of secreted gelatin and Yps1-mediated alpha-factor leader processing in a Pichia pastoris kex2 disruptant.Appl Environ Microbiol. 2005 May;71(5):2310-7. doi: 10.1128/AEM.71.5.2310-2317.2005. Appl Environ Microbiol. 2005. PMID: 15870316 Free PMC article.
-
Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.EMBO Rep. 2003 Oct;4(10):937-8. doi: 10.1038/sj.embor.embor946. EMBO Rep. 2003. PMID: 14528262 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
