Abstract
BackgroundThe Myb super-family of proteins contain a group of functionally diverse transcriptional activators found in plant, animal and fungus. Myb proteins are involved in cell proliferation, differentiation and apoptosis, and have crucial roles in telomeres. The purpose of this study was to characterize the biological function of Myb1 protein in the rice blast fungus Magnaporthe oryzae.ResultsWe identified the Saccharomyces cerevisiae BAS1 homolog MYB1 in M. oryzae, named MoMyb1. MoMyb1 encodes a protein of 322 amino acids and has two SANT domains and is well conserved in various organisms. Targeted gene deletion of MoMYB1 resulted in a significant reduction in vegetative growth and showed defects in conidiation and conidiophore development. Quantitative RT-PCR analysis revealed that the transcription levels of several conidiophore-related genes were apparently decreased in the ΔMomyb1 mutant. Inoculation with mycelia mats displayed that the virulence of the ΔMomyb1 mutant was not changed on rice leaves but was non-pathogenic on rice roots in comparison to the wild type Guy11. In addition, ∆Momyb1 mutants showed increased resistance to osmotic stresses but more sensitive to cell wall stressor calcofluor white (CFW). Further analysis revealed that MoMyb1 has an important role in the cell wall biosynthesis pathway.ConclusionThis study provides the evidence that MoMyb1 is a key regulator involved in conidiogenesis, stress response, cell wall integrity and pathogenesis on rice roots in the filamentous phytopathogen M. oryzae.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-015-0375-y) contains supplementary material, which is available to authorized users.
Highlights
The Myb super-family of proteins contain a group of functionally diverse transcriptional activators found in plant, animal and fungus
Identification of M. oryzae MYB1 The Myb family of proteins is a group of functionally diverse transcriptional activators that is characterized by a conserved Desoxyribonucleic acid (DNA)-binding domain of approximately 50 amino acids [14]
We conclude that MoMyb1 is a key regulator of M. oryzae for conidium and conidiophore development. quantitative RT-PCR (qRT-PCR) analysis revealed the expression level of five conidiogenesisrelated genes were significantly decreased in the ΔMomyb1 mutant, indicating that MoMyb1 probably functions as a key upstream transcription factor in the conidiogenesis signalling pathway to regulate the expression of genes which involved in conidiophore and conidium development
Summary
The Myb super-family of proteins contain a group of functionally diverse transcriptional activators found in plant, animal and fungus. The purpose of this study was to characterize the biological function of Myb protein in the rice blast fungus Magnaporthe oryzae. Regulation of gene expression at the level of transcription controls many crucial biological processes. Transcription factors can recognize DNA in a sequence-specific manner and modulate the frequency of initiation of transcription upon binding to specific sites in the promoter of target genes. The transcription factors can be activators, repressors, or both usually display a modular structure named the DNA-binding domain [5]. In M. oryzae, numerous transcription factors were identified and characterized to be important for proper regulation of infection related morphogenesis [6,7]. Many transcription factors, including MoCrz, MoAp1, MoAtf, MoHac, MoBzip, MoSwi and MoMsn were reported to be involved in hyphal growth, asexual
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