التفاصيل البيبلوغرافية
| العنوان: |
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. |
| المؤلفون: |
Sepúlveda-González, Mª Eugenia, Parra-Ortega, Berenice, Betancourt-Cervantes, Yuliana, Hernández-Rodríguez, César, Xicohtencatl-Cortes, Juan, Villa-Tanaca, Lourdes |
| المصدر: |
Revista Iberoamericana de Micologia; Jan-Mar2016, Vol. 33 Issue 1, p26-33, 8p |
| مصطلحات موضوعية: |
CARBOXYPEPTIDASES, AMINO acid sequence, NEUTRAL proteinases, YEAST, MICROSCOPY, NITROGEN |
| الملخص (بالإنجليزية): |
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. [ABSTRACT FROM AUTHOR] |
| Abstract (Spanish): |
Resumen Antecedentes La vacuola de Saccharomyces cerevisiae está involucrada activamente en el mecanismo de autofagia, desarrollando una labor importante en la homeostasis, degradación, recambio proteico, desintoxicación y protección de la célula en condiciones de estrés. Por el contrario, las proteasas vacuolares de Candida glabrata aún no han sido estudiadas por completo. Objetivos El presente trabajo describe por primera vez la actividad proteolítica vacuolar en C. glabrata . Métodos Los estudios bioquímicos realizados en C. glabrata pusieron de manifiesto la presencia de diferentes actividades proteolíticas: aspartil proteinasa ácida, que actúa sobre sustratos como la albúmina y la hemoglobina ácida desnaturalizada; serín proteasa neutra, con actividad sobre el substrato de tipo colágeno hide powder azure , y serín carboxipeptidasa, que actúa sobre N-benzoil-tyr-pNa. Resultados La obtención de una fracción subcelular mostró una elevada actividad enzimática específica de las tres proteasas, lo que permitió confirmar su localización vacuolar. Se realizaron análisis de la expresión de los genes CgPEP4 (CgAPR1) , CgPRB1 y CgCPY1 (CgPRC1) , codificantes de las actividades proteolíticas aspartil proteasa A, proteasa neutra B y carboxipeptidasa Y, respectivamente. Los resultados reflejan una regulación diferencial de la expresión de la proteasa, dependiendo de la fuente de nitrógeno. Conclusiones Las proteasas codificadas por los genes CgPEP4 , CgPRB1 y CgCPY1 podrían participar en el proceso de autofagia y supervivencia de este patógeno oportunista. [ABSTRACT FROM AUTHOR] |
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