In the recent publication by Wang et al. HUABIO’s anti-RPS3 antibody and anti-RPS20 antibody helped determine if FgRbp1 is a splicing regulator and regulates the pre-mRNA splicing in a sequence-dependent manner in F. graminearum.
Fusarium graminearum is the predominant causal agent of Fusarium head blight (FHB), an economically devastating disease of small grain cereal crops worldwide. These species are rank pathogens, invading plants and grains by causing diseases, known as Gibberella ear rot in maize and Fusarium head blight in wheat, barley, and triticale.
RNA-binding proteins (RBPs) are critical for co-transcriptional and post-transcriptional gene expression in eukaryotic organisms. Many RBPs are characterized by the presence of various RNA-binding domains including the RNA recognition motif (RRM), K-homology (KH) domain, the zinc finger domain, the DEAD-box domain, and the Pumilio/FBF domain.
Precursor messenger RNA (pre-mRNA) splicing is an essential and tightly regulated process in eukaryotic cells; however, the regulatory mechanisms for the splicing are not well understood. Wang et al. characterize a RNA binding protein named FgRbp1 in Fusarium graminearum, a fungal pathogen of cereal crops worldwide. Deletion of FgRbp1 leads to reduced splicing efficiency in 47% of the F. graminearum intron-containing gene transcripts that are involved in various cellular processes including vegetative growth, development, and virulence. The human ortholog RBM42 is able to fully rescue the growth defects of ΔFgRbp1. FgRbp1 binds to the motif CAAGR in its target mRNAs, and interacts with the splicing factor FgU2AF23, a highly conserved protein involved in 3’ splice site recognition, leading to enhanced recruitment of FgU2AF23 to the target mRNAs. This study demonstrates that FgRbp1 is a splicing regulator and regulates the pre-mRNA splicing in a sequence-dependent manner in F. graminearum.