-
Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis.
Service de Dermatologie, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
The extracellular acid protease of Candida tropicalis was purified from the supernatant fraction of culture medium containing bovine serum albumin as nitrogen source and the NH2-terminal amino acid (aa) sequence of the protein was determined. The gene for the acid protease (ACP) was isolated using a pool of synthetic oligonucleotides as a probe and a segment of the deduced aa sequence was found to be in agreement with the NH2-terminal aa sequence of the protein. The deduced aa sequence of ACP is similar to the aa sequence of proteases of the pepsin family. The nucleotide sequence of the 5' portion of this gene revealed a coding sequence for a 60 residue propeptide containing two Lys-Arg amino acid pairs that have been identified as sites for peptidase processing of several exported peptides and proteins. The final Lys-Arg site occurs at the junction with the mature extracellular form of the acid protease.
PMID: 1864366 [PubMed - indexed for MEDLINE]
-
Cited by 13 PubMed Central articles
-
ReviewCandida albicans secreted aspartyl proteinases in virulence and pathogenesis.
Naglik JR, Challacombe SJ, Hube B.
Microbiol Mol Biol Rev. 2003 Sep; 67(3):400-28, table of contents.
[Microbiol Mol Biol Rev. 2003]
-
Secreted aspartic proteinase family of Candida tropicalis.
Zaugg C, Borg-Von Zepelin M, Reichard U, Sanglard D, Monod M.
Infect Immun. 2001 Jan; 69(1):405-12.
[Infect Immun. 2001]
-
ReviewMolecular and biotechnological aspects of microbial proteases.
Rao MB, Tanksale AM, Ghatge MS, Deshpande VV.
Microbiol Mol Biol Rev. 1998 Sep; 62(3):597-635.
[Microbiol Mol Biol Rev. 1998]
- » See all...