Vacuolar proteases from Candida glabrata: Acid aspartic protease PrA, neutral serine protease PrB and serine carboxypeptidase CpY. The nitrogen source influences their level of expression

详细信息    查看全文

• 作者：M&ordf ; Eugenia Sepú ; lveda-Gonzá ; lez^a ; ^b ; Berenice Parra-Ortega^a ; Yuliana Betancourt-Cervantes^a ; Cé ; sar Herná ; ndez-Rodrí ; guez^a ; Juan Xicohtencatl-Cortes^b ; ^{juanxico@yahoo.com" class="auth_mail" title="E-mail the corresponding author} ; Lourdes Villa-Tanaca^a ; ^{lourdesvilla@hotmail.com" class="auth_mail" title="E-mail the corresponding author} ; ^{mvillat@ipn.mx" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Proteases ; Vacuole ; Candida glabrata ; Autophagy
• 刊名：Revista Iberoamericana de Micología
• 出版年：2016
• 出版时间：January-March 2016
• 年：2016
• 卷：33
• 期：1
• 页码：26-33
• 全文大小：1638 K

文摘

The m>Saccharomyces cerevisiaem> vacuole is actively involved in the mechanism of autophagy and is important in homeostasis, degradation, turnover, detoxification and protection under stressful conditions. In contrast, vacuolar proteases have not been fully studied in phylogenetically related m>Candida glabratam>.

Aims

The present paper is the first report on proteolytic activity in the m>C. glabratam> vacuole.

Methods

Biochemical studies in m>C. glabratam> have highlighted the presence of different kinds of intracellular proteolytic activity: acid aspartyl proteinase (PrA) acts on substrates such as albumin and denatured acid hemoglobin, neutral serine protease (PrB) on collagen-type hide powder azure, and serine carboxypeptidase (CpY) on N-benzoyl-tyr-pNA.

Results

Our results showed a subcellular fraction with highly specific enzymatic activity for these three proteases, which allowed to confirm its vacuolar location. Expression analyses were performed in the genes m>CgPEP4 (CgAPR1)m>, m>CgPRB1m> and m>CgCPY1 (CgPRC)m>, coding for vacuolar aspartic protease A, neutral protease B and carboxypeptidase Y, respectively. The results show a differential regulation of protease expression depending on the nitrogen source.

Conclusions

The proteases encoded by genes m>CgPEP4m>, m>CgPRB1m> and m>CgCPY1m> from m>C. glabratam> could participate in the process of autophagy and survival of this opportunistic pathogen.