title: Light-dependent roles of the G-protein alpha subunit GNA1 of Hypocrea jecorina (anamorph Trichoderma reesei).
abstract: BACKGROUND
  The filamentous ascomycete Hypocrea jecorina (anamorph Trichoderma reesei) is primarily known for its efficient enzymatic machinery that it utilizes to decompose cellulosic substrates. Nevertheless, the nature and transmission of the signals initiating and modulating this machinery are largely unknown. Heterotrimeric G-protein signaling represents one of the best studied signal transduction pathways in fungi.
  
  
  RESULTS
  Analysis of the regulatory targets of the G-protein alpha subunit GNA1 in H. jecorina revealed a carbon source and light-dependent role in signal transduction. Deletion of gna1 led to significantly decreased biomass formation in darkness in submersed culture but had only minor effects on morphology and hyphal apical extension rates on solid medium. Cellulase gene transcription was abolished in Deltagna1 on cellulose in light and enhanced in darkness. However, analysis of strains expressing a constitutively activated GNA1 revealed that GNA1 does not transmit the essential inducing signal. Instead, it relates a modulating signal with light-dependent significance, since induction still required the presence of an inducer. We show that regulation of transcription and activity of GNA1 involves a carbon source-dependent feedback cycle. Additionally we found a function of GNA1 in hydrophobin regulation as well as effects on conidiation and tolerance of osmotic and oxidative stress.
  
  
  CONCLUSIONS
  We conclude that GNA1 transmits a signal the physiological relevance of which is dependent on both the carbon source as well as the light status. The widespread consequences of mutations in GNA1 indicate a broad function of this Galpha subunit in appropriation of intracellular resources to environmental (especially nutritional) conditions.
authors.affiliation: Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Wien, Austria. christian.seibel@tuwien.ac.at
authors.forename: Christian
authors.initials: C
authors.lastname: Seibel
authors.forename: Gabriela
authors.initials: G
authors.lastname: Gremel
authors.forename: Roberto
authors.initials: R
authors.lastname: do Nascimento Silva
authors.forename: André
authors.initials: A
authors.lastname: Schuster
authors.forename: Christian P
authors.initials: CP
authors.lastname: Kubicek
authors.forename: Monika
authors.initials: M
authors.lastname: Schmoll
mesh_terms: D002244:Carbon / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D003624:Darkness; D025461:Feedback, Physiological; D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology*; D044385:GTP-Binding Protein alpha Subunits / Q000235:genetics / Q000502:physiology*; D017353:Gene Deletion; D015966:Gene Expression Regulation, Fungal; D005947:Glucose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D035901:Hypocrea / Q000737:chemistry / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D008027:Light; D016296:Mutagenesis; D009997:Osmotic Pressure; D018384:Oxidative Stress; D011994:Recombinant Proteins / Q000378:metabolism; D015398:Signal Transduction; D024483:Vitamin K 3 / Q000633:toxicity
chemical_list: D005656:Fungal Proteins; D044385:GTP-Binding Protein alpha Subunits; D011994:Recombinant Proteins; D024483:Vitamin K 3; D002244:Carbon; D002482:Cellulose; D043366:Cellulose 1,4-beta-Cellobiosidase; D005947:Glucose; D005990:Glycerol