Volume 36, Issue 11 pp. 1207-1216
Article
Free Access

cDNA Cloning of an Aspartic Proteinase Secreted by Candida albicans

Hiroyuki Mukai

Hiroyuki Mukai

Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Ohtsu, Shiga, 520-21 Japan

Search for more papers by this author
Osamu Takeda

Osamu Takeda

Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Ohtsu, Shiga, 520-21 Japan

Search for more papers by this author
Kiyozo Asada

Kiyozo Asada

Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Ohtsu, Shiga, 520-21 Japan

Search for more papers by this author
Ikunoshin Kato

Ikunoshin Kato

Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Ohtsu, Shiga, 520-21 Japan

Search for more papers by this author
Somay Yamagata Murayama

Somay Yamagata Murayama

Department of Bacteriology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, 173 Japan

Search for more papers by this author
Hideyo Yamaguchi

Hideyo Yamaguchi

Department of Bacteriology, Teikyo University School of Medicine, Itabashi-ku, Tokyo, 173 Japan

Teikyo University Research Center for Medical Mycology, Hachioji, Tokyo, 192-03 Japan

Search for more papers by this author
First published: November 1992
Citations: 7

Abstract

cDNA of an aspartic proteinase secreted by Candida albicans No. 114 was isolated using the polymerase chain reaction (PCR). The primary structure of the enzyme was deduced from the nucleotide sequence of the cDNA and compared with the structures of Saccharomyces cerevisiae proteinase A and vacuolar aspartyl proteinase of C. albicans. The mature aspartic proteinase consisted of 341 amino acid residues, and was 17.6 and 15.3% identical with the proteinase A and the aspartyl proteinase, respectively. Two active aspartic acid sites and the amino acids near those sites were conserved in the aspartic proteinase. We also showed that there is another gene of aspartic proteinase than that of strain ATCC10231 reported by Hube et al (J. Med. Vet. Mycol. 29 (1991)) in the same C. albicans genome, both in that strain and in No. 114.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.