Analysis of the phosphorylome of trichoderma reesei cultivated on sugarcane bagasse suggests post-translational regulation of the secreted glycosyl hydrolase Cel7A

Biotechnology Reports

Amanda Cristina Campos Antoniêto¹  Cláudia Batista Carraro²  David Batista Maués²  Iasmin Cartaxo Taveira²  André Ricardo de Lima Damasio²  Maíra Pompeu Martins²  Renato Graciano de Paula²  Rafael Silva-Rocha³  Liliane Fraga Costa Ribeiro⁴  Wellington Ramos Pedersoli⁴  Roberto N Silva⁴  Antônio Rossi Filho⁵ 

[1] Department of Physiological Sciences, Health Sciences Centre, Federal University of Espirito Santo, Vitória, ES, 29047-105, Brazil;Department of Biochemistry and Immunology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, 14049-900, Brazil;Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas (UNICAMP), Campinas, SP, 13083-970, Brazil;Department of Genetics, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, 14049-900, Brazil;Systems and Synthetic Biology Laboratory, Department of Cell and Molecular Biology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, 14049-900, Brazil;

关键词: Trichoderma reesei;    Phosphorylome;    Sugarcane bagasse;    Cel7A;    Phosphorylation;   

DOI  :  

来源: DOAJ

【 摘 要 】

Trichoderma reesei is one of the major producers of holocellulases. It is known that in T. reesei, protein production patterns can change in a carbon source-dependent manner. Here, we performed a phosphorylome analysis of T. reesei grown in the presence of sugarcane bagasse and glucose as carbon source. In presence of sugarcane bagasse, a total of 114 phosphorylated proteins were identified. Phosphoserine and phosphothreonine corresponded to 89.6% of the phosphosites and 10.4% were related to phosphotyrosine. Among the identified proteins, 65% were singly phosphorylated, 19% were doubly phosphorylated, 12% were triply phosphorylated, and 4% displayed even higher phosphorylation. Seventy-five kinases were predicted to phosphorylate the sites identified in this work, and the most frequently predicted serine/threonine kinase was PKC1. Among phosphorylated proteins, four glycosyl hydrolases were predicted to be secreted. Interestingly, Cel7A activity, the most secreted protein, was reduced to approximately 60% after in vitro dephosphorylation, suggesting that phosphorylation might alter Cel7A structure, substrate affinity, and targeting of the substrate to its carbohydrate-binding domain. These results suggest a novel post-translational regulation of Cel7A.

【 授权许可】

Unknown