Proteomic analysis of the signaling pathway mediated by the heterotrimeric Gα protein Pga1 of Penicillium chrysogenum

Microbial Cell Factories

Research

Francisco Fierro¹  Eduardo Zúñiga-León¹  Ulises Carrasco-Navarro¹  Francisco J. Fernández¹  Rosario Vera-Estrella²  Horacio Reyes-Vivas³  Bronwyn J. Barkla⁴ 

[1] Departamento de Biotecnología, Universidad Autónoma Metropolitana-Unidad Iztapalapa, México D.F., México;Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México;Laboratorio de Bioquímica-Genética, Instituto Nacional de Pediatría, Secretaría de Salud, México D.F., México;Southern Cross Plant Science, Southern Cross University, Lismore, NSW, Australia;

关键词: Penicillium chrysogenum;    Pga1 Gα subunit;    Signal transduction;    Heterotrimeric G protein;    Proteomics;    Penicillin biosynthesis;   

DOI  :  10.1186/s12934-016-0564-x

 received in 2016-06-21, accepted in 2016-09-21,  发布年份 2016

来源: Springer

【 摘 要 】

BackgroundThe heterotrimeric Gα protein Pga1-mediated signaling pathway regulates the entire developmental program in Penicillium chrysogenum, from spore germination to the formation of conidia. In addition it participates in the regulation of penicillin biosynthesis. We aimed to advance the understanding of this key signaling pathway using a proteomics approach, a powerful tool to identify effectors participating in signal transduction pathways.ResultsPenicillium chrysogenum mutants with different levels of activity of the Pga1-mediated signaling pathway were used to perform comparative proteomic analyses by 2D-DIGE and LC–MS/MS. Thirty proteins were identified which showed differences in abundance dependent on Pga1 activity level. By modifying the intracellular levels of cAMP we could establish cAMP-dependent and cAMP-independent pathways in Pga1-mediated signaling. Pga1 was shown to regulate abundance of enzymes in primary metabolic pathways involved in ATP, NADPH and cysteine biosynthesis, compounds that are needed for high levels of penicillin production. An in vivo phosphorylated protein containing a pleckstrin homology domain was identified; this protein is a candidate for signal transduction activity. Proteins with possible roles in purine metabolism, protein folding, stress response and morphogenesis were also identified whose abundance was regulated by Pga1 signaling.ConclusionsThirty proteins whose abundance was regulated by the Pga1-mediated signaling pathway were identified. These proteins are involved in primary metabolism, stress response, development and signal transduction. A model describing the pathways through which Pga1 signaling regulates different cellular processes is proposed.

【 授权许可】

CC BY   
© The Author(s) 2016