AoSO protein accumulates at the septal pore in response to various stresses in the filamentous fungus Aspergillus oryzae

Maruyama, Jun‐ichi; Escaño, Cristopher Salazar; Kitamoto, Katsuhiko

doi:10.1016/j.bbrc.2009.11.154

Cited by 37 publications

(47 citation statements)

References 18 publications

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“…SOFT is a cytoplasmic protein required for fungal cell-to-cell fusion, which has previously been localized to septal pore plugs (32,33). The N-terminal domain of SOFT is predicted to be disordered (Fig.…”

Section: Discussionmentioning

confidence: 99%

Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity

Lai

Koh

Tjota

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Like animals and plants, multicellular fungi possess cell-to-cell channels (septal pores) that allow intercellular communication and transport. Here, using a combination of MS of Woronin bodyassociated proteins and a bioinformatics approach that identifies related proteins based on composition and character, we identify 17 septal pore-associated (SPA) proteins that localize to the septal pore in rings and pore-centered foci. SPA proteins are not homologous at the primary sequence level but share overall physical properties with intrinsically disordered proteins. Some SPA proteins form aggregates at the septal pore, and in vitro assembly assays suggest aggregation through a nonamyloidal mechanism involving mainly α-helical and disordered structures. SPA loss-of-function phenotypes include excessive septation, septal pore degeneration, and uncontrolled Woronin body activation. Together, our data identify the septal pore as a complex subcellular compartment and focal point for the assembly of unstructured proteins controlling diverse aspects of intercellular connectivity. multicellular organization | filamentous fungus | Neurospora crassa

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Section: Discussionmentioning

confidence: 99%

Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity

Lai

Koh

Tjota

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…All of the primers used in this study are listed in Supplemental Table 1 Construction of the pyrG and adeB disruptants. For disruption of pyrG and adeB genes, the wild-type strain NSRKu70-1-1A 29) and ΔAoso strain 25,26) were used as hosts. In order to generate ΔAoso strain, the 1.5-kb upstream flanking region of the Aofus3 ORF (AO090003000402) was amplified with the primers (fus3-5UTR-F and fus3-5UTR-adeA-R) and the genomic DNA as template.…”

Section: )mentioning

confidence: 99%

“…19−21) In Aspergillus nidulans, AnFus3/ MpkB homologous to N. crassa MAK-2 is required for hyphal fusion and sexual development. 22−24) AoSO protein homologous to N. crassa SO accumulates at the septal pore in response to various stresses, 25) and it colocalizes with stress granules. 26) However, functional involvement of AoSO in hyphal fusion has not been investigated since an effective assay of hyphal fusion efficiency has been lacking in A. oryzae.…”

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confidence: 99%

Establishment of a new method to quantitatively evaluate hyphal fusion ability in Aspergillus oryzae

Tsukasaki

Maruyama

Kitamoto

2014

Bioscience, Biotechnology, and Biochemistry

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Hyphal fusion is involved in the formation of an interconnected colony in filamentous fungi, and it is the first process in sexual/parasexual reproduction. However, it was difficult to evaluate hyphal fusion efficiency due to the low frequency in Aspergillus oryzae in spite of its industrial significance. Here, we established a method to quantitatively evaluate the hyphal fusion ability of A. oryzae with mixed culture of two different auxotrophic strains, where the ratio of heterokaryotic conidia growing without the auxotrophic requirements reflects the hyphal fusion efficiency. By employing this method, it was demonstrated that AoSO and AoFus3 are required for hyphal fusion, and that hyphal fusion efficiency of A. oryzae was increased by depleting nitrogen source, including large amounts of carbon source, and adjusting pH to 7.0.

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“…However, So orthologs are large proteins with an estimated molecular mass of 140 kDa (10) and may have multiple molecular functions. Indeed, the So orthologs have also been implicated in the plugging of septal pores in aging hyphae or after hyphal injury (10,16,24). It is currently unknown whether this function of So orthologs is associated with their role in hyphal anastomosis.…”

Section: Discussionmentioning

confidence: 99%

Deletion of the Fungal Gene soft Disrupts Mutualistic Symbiosis between the Grass Endophyte Epichloë festucae and the Host Plant

et al. 2012

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Hyphal anastomosis, or vegetative hyphal fusion, establishes the interconnection of individual hyphal strands into an integrated network of a fungal mycelium. In contrast to recent advances in the understanding of the molecular basis for hyphal anastomosis, knowledge of the physiological role of hyphal anastomosis in the natural habitats of filamentous fungi is still very limited. To investigate the role of hyphal anastomosis in fungal endophyte-plant interactions, we generated mutant strains lacking the Epichloë festucae soft (so) gene, an ortholog of the hyphal anastomosis gene so in the endophytic fungus E. festucae. The E. festucae ⌬so mutant strains grew similarly to the wild-type strain in culture but with reduced aerial hyphae and completely lacked hyphal anastomosis. The most striking phenotype of the E. festucae ⌬so mutant strain was that it failed to establish a mutualistic symbiosis with the tall fescue plant host (Lolium arundinaceum); instead, it killed the host plant within 2 months after the initial infection. Microscopic examination revealed that the death of the tall fescue plant host was associated with the distortion and disorganization of plant cells. This study suggests that hyphal anastomosis may have an important role in the establishment/ maintenance of fungal endophyte-host plant mutualistic symbiosis.

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AoSO protein accumulates at the septal pore in response to various stresses in the filamentous fungus Aspergillus oryzae

Cited by 37 publications

References 18 publications

Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity

Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity

Establishment of a new method to quantitatively evaluate hyphal fusion ability in Aspergillus oryzae

Deletion of the Fungal Gene soft Disrupts Mutualistic Symbiosis between the Grass Endophyte Epichloë festucae and the Host Plant

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