MoTea4-mediated polarized growth is essential for proper asexual development and pathogenesis in Magnaporthe oryzae.
Polarized growth is essential for cellular development and function and requires coordinated organization of the cytoskeletal elements. Tea4, an important polarity determinant, regulates localized F-actin assembly and bipolar growth in fission yeast and directional mycelial growth in Aspergillus. Here, we characterize Tea4 in the rice blast fungus Magnaporthe oryzae (MoTea4). Similar to its orthologs, MoTea4-green fluorescent protein (MoTea4-GFP) showed punctate distribution confined to growth zones, particularly in the mycelial tips, aerial hyphae, conidiophores, conidia, and infection structures (appressoria) in Magnaporthe. MoTea4 was dispensable for vegetative growth in Magnaporthe. However, loss of MoTea4 led to a zigzag morphology in the aerial hyphae and a huge reduction in conidiation. The majority of the tea4Delta conidia were two celled, as opposed to the tricellular conidia in the wild type. Structure-function analysis indicated that the SH3 and coiled-coil domains of MoTea4 are necessary for proper conidiation in Magnaporthe. The tea4Delta conidia failed to produce proper appressoria and consequently failed to infect the host plants. The tea4Delta conidia and germ tubes showed disorganized F-actin structures with significantly reduced numbers of cortical actin patches. Compared to the wild-type conidia, the tea4Delta conidia showed aberrant germination, poor cytoplasmic streaming, and persistent accumulation of lipid droplets, likely due to the impaired F-actin cytoskeleton. Latrunculin A treatment of germinating wild-type conidia showed that an intact F-actin cytoskeleton is indeed essential for appressorial development in Magnaporthe. We show that MoTea4 plays an important role in organizing the F-actin cytoskeleton and is essentially required for polarized growth and morphogenesis during asexual and pathogenic development in Magnaporthe.
Patkar
Rajesh N
RN
Fungal Patho-Biology Group, Temasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore 117604, Republic of Singapore.
Suresh
Angayarkanni
A
Naqvi
Naweed I
NI
D000199:Actins / Q000378:metabolism; D016764:Cell Polarity; D003595:Cytoplasmic Streaming; D003599:Cytoskeleton / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D017353:Gene Deletion; D049452:Green Fluorescent Proteins / Q000378:metabolism; D020082:Magnaporthe / Q000166:cytology / Q000254:growth & development* / Q000472:pathogenicity*; D008869:Microtubule-Associated Proteins / Q000737:chemistry; D010641:Phenotype; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012100:Reproduction, Asexual / Q000502:physiology*; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions / Q000378:metabolism; D014774:Virulence
D000199:Actins; D005656:Fungal Proteins; D008869:Microtubule-Associated Proteins; D011993:Recombinant Fusion Proteins; D029702:Schizosaccharomyces pombe Proteins; C501888:Tea4 protein, S pombe; D049452:Green Fluorescent Proteins
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