TY - JOUR
T1 - Vacuolar proteases from Candida glabrata
T2 - Acid aspartic protease PrA, neutral serine protease PrB and serine carboxypeptidase CpY. The nitrogen source influences their level of expression
AU - Sepúlveda-González, M. Eugenia
AU - Parra-Ortega, Berenice
AU - Betancourt-Cervantes, Yuliana
AU - Hernández-Rodríguez, César
AU - Xicohtencatl-Cortes, Juan
AU - Villa-Tanaca, Lourdes
N1 - Publisher Copyright:
© 2014 Asociación Española de Micología.
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Background: The Saccharomyces cerevisiae 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 Candida glabrata. Aims: The present paper is the first report on proteolytic activity in the C. glabrata vacuole. Methods: Biochemical studies in C. glabrata 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 CgPEP4 (CgAPR1), CgPRB1 and CgCPY1 (CgPRC), 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 CgPEP4, CgPRB1 and CgCPY1 from C. glabrata could participate in the process of autophagy and survival of this opportunistic pathogen.
AB - Background: The Saccharomyces cerevisiae 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 Candida glabrata. Aims: The present paper is the first report on proteolytic activity in the C. glabrata vacuole. Methods: Biochemical studies in C. glabrata 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 CgPEP4 (CgAPR1), CgPRB1 and CgCPY1 (CgPRC), 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 CgPEP4, CgPRB1 and CgCPY1 from C. glabrata could participate in the process of autophagy and survival of this opportunistic pathogen.
KW - Autophagy
KW - Candida glabrata
KW - Proteases
KW - Vacuole
UR - http://www.scopus.com/inward/record.url?scp=84962019801&partnerID=8YFLogxK
U2 - 10.1016/j.riam.2014.10.005
DO - 10.1016/j.riam.2014.10.005
M3 - Artículo
C2 - 26422323
SN - 1130-1406
VL - 33
SP - 26
EP - 33
JO - Revista Iberoamericana de Micologia
JF - Revista Iberoamericana de Micologia
IS - 1
ER -