A. oryzae
not annotated - annotated - LINNAEUS only
22008745
Identification and characterization of a putative basic helix-loop-helix transcription factor involved in the early stage of conidiophore development in Aspergillus oryzae.
The helix-loop-helix (HLH) family of transcriptional factors is a key player in a wide range of developmental processes. HLH proteins form homo- and/or heterodimers with other HLH proteins and bind to E-box motifs. The regulation and functions of these proteins can be complex due to their bifunctional roles as activators and repressors of gene transcription. In this study, we isolated and characterized a novel predicted bHLH protein-encoding gene, AO090023000902, designated ecdR (early conidiophore development regulator), in Aspergillus oryzae. The ecdR gene disruptant produced very few conidia. Conversely, the overexpression of ecdR resulted in the formation of a large number of conidia at an early stage, suggesting that the EcdR protein is required for early asexual development. Additionally, when serially diluted conidia were spread-cultivated onto malt agar medium, we found that conidial number of the control strain depended on the cultivated conidium density, while the ecdR-overexpressing strain showed no significant change in conidiation. These phenotypes of ecdR-disruptant and ecdR-overexpressing strains are partially similar to those of the sclR-overexpressing strain and sclR-disruptant, respectively. Yeast two-hybrid assays and sclR, ecdR-double deletion experiment indicated that EcdR plays a major role in conidiation, and SclR represses this function by competitively interacting with EcdR in A. oryzae.
21277379
Independent duplications of alpha-amylase in different strains of Aspergillus oryzae.
Aspergillus oryzae is a filamentous fungus that has arisen through the ancient domestication of Aspergillus flavus for making traditional oriental foods and beverages. In the many centuries A. oryzae has been used for fermenting the starch in rice to simple sugars, it has undergone selection for increased secretion of starch-degrading enzymes. In particular, all A. oryzae strains investigated thus far have two or more copies of a gene encoding alpha-amylase, whereas A. flavus has only one. Here we investigate the duplications leading to these copies in three A. oryzae strains. We find evidence of at least three separate duplications of alpha-amylase, an example of parallel evolution in a micro-organism under artificial selection. At least two of these duplications appear to be associated with activity of transposable elements of the Tc1/mariner class. Both involve a 9.1 kb element that terminates in inverted repeats, encodes a putative transposase and another putative protein of unknown function, and contains an unusual arrangement of four short internal imperfect repeats. Although "unusual Mariners" of this size have previously been identified in A. oryzae, Aspergillus fumigatus and Aspergillus nidulans, this is the first evidence we know of that at least some of them are active in modern times and that their activity can contribute to beneficial genetic changes.