A Component of the Septation Initiation Network Complex, SepL, Participates in the Cellobiose-Responsive Expression of Cellulolytic Enzyme Genes in Aspergillus aculeatus.

The production of cellulolytic enzymes in Aspergillus aculeatus is regulated at transcriptional levels in response to inducers and various physiological signals. In this study, we identified that a component of the septation initiation network complex, SepL, a putative protein kinase, was involved in the expression of carbohydrate-active enzyme (CAZyme) encoding genes. The deletion of sepL (ΔsepL) in A. aculeatus resulted in a deficiency in both septation and conidiation and sensitivity to Congo red. These phenotypes of ΔsepL are conserved in Aspergillus. In addition to the conserved function of SepL in Aspergillus, we found that SepL in A. aculeatus was necessary for the inducible expression of the CAZyme genes in response to cellobiose, whereas the inducible expression of these genes in response to 1,4-β-mannobiose was significantly reduced but not abolished. Combining the results of the present functional analysis of SepL with previous evidence that the expression of the CAZyme genes, which is responsive to both cellobiose and 1,4-β-mannobiose, is regulated by a transcription factor ManR in A. aculeatus, indicates that SepL in A. aculeatus is involved in the selective expression of the cellobiose-responsive CAZyme genes under the control of ManR.