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Studies on regulatory mechanisms of cell-to-cell communication in multicellularity of the filamentous fungus Aspergillus oryzae

MAMUN, MD. ABDULLA AL 東京大学 DOI:10.15083/0002004924

2022.06.22

概要

Introduction
The emergence of multicellularity is an important transition in history of life on earth. The unicellular organisms evolved their genome structures and modified their morphological identities into a cell community for better mutual cooperation, which generated the organisms as multicellular. Gap junction and plasmodesmata are the major channels of cell-to-cell communication in animal and plant, respectively. Fungi contain both unicellular and multicellular species and could be considered as a good eukaryotic model for multicellularity study

Pezizomycotina species under the Ascomycota, one of fungal divisions, possess a primitive morphological structure for cell-to-cell communication in fungal multicellular organization. In vegetative phase, after hyphae grow a certain length with several nuclear divisions, a cross wall called septum (equivalent to cytokinesis) is formed by deposition of cell wall. In Pezizomycotina, septum formation is distinct from ascomycete yeast by retaining a septal pore at the center of septum, which allows exchange of cytoplasmic constituents between the flanking cells. Due to the porous septum morphology, Pezizomycotina are highly vulnerable to the risk of uncontrolled cytoplasmic loss via the septal pore upon hyphal wounding. A Pezizomycotina-specific organelle Woronin body plugs the septal pore and protects the adjacent cells from excessive loss of cytoplasm. Additionally, the septal pore is closed to block the communication between the flanking cells during mitosis.

Septal pore is highly dynamic, and the regulation involves complex mechanisms. Previously, genetic approach was employed to explore the components involved in septal pore-based multicellularity. However, comparative genomic approach between multicellular and unicellular fungal species has not yet been employed to investigate additional components/mechanisms in the regulation of cell-to-cell communication. In the thesis, I performed a genomic comparison between multicellular and unicellular ascomycetes as Ascomycota possesses a number of genetically well-analyzed species, and subsequent localization screening of the selected proteins to find novel components regulating the cell-to-cell communication via septal pore. In this study, I used Aspergillus oryzae due to having a unique experiment system of quantitatively analyzing the ability to protect the flanking cells upon hypotonic shock-induced hyphal wounding, which reflects septal pore states or Woronin body function.

Chapter 1: Identification of a novel Pezizomycotina-specific actin regulator for septum formation
Fungal septum formation is commonly regulated by contractile actin ring, whereas Pezizomycotina species do not completely divide the cells by the retention of septal pore, which mechanistically differs from complete separation of daughter cells in unicellular ascomycete yeasts. For finding a Pezizomycotina-specific actin regulator, I designed a screening strategy based on bioinformatics tools. Firstly, gene ontology (GO) terms for actin were employed for selecting candidate actin regulators from A. oryzae genome database. Secondly, based on protein BLAST, I preferentially selected genes conserved in Pezizomycotina but not conserved in ascomycete yeasts and got three genes. After excluding functionally characterized two, the finally selected gene encodes a protein containing three gelsolin domains. The gene was designated as glpA (for gelsolin-like protein) and encodes a protein of 1837 amino acids. Gelsolin is generally known as an actin-modulating protein with severing activity. Phylogenetic analysis showed that GlpA forms as a Pezizomycotina-specific clade with other orthologues from multicellular fungal species.

Gene deletion strain of glpA was generated for observing septum formation phenotype. glpA deletion resulted in infrequent septum formation as supported by the abnormally increased distances of hyphal cells. Approximately 70% of the septa were found to be morphologically abnormal in ΔglpA. Septal pore function in ΔglpA was analyzed by hypotonic shock-induced hyphal tip bursting. It was reported that Woronin body protects the hyphae from excessive loss of cytoplasm at the adjacent second cell upon hyphal tip bursting. Wild type showed 84% ability to prevent the cytoplasmic loss, while ΔglpA showed only 13% ability comparable to that of Woronin body-deficient ΔAohex1 (18%). The regulation of septal pores in ΔglpA under stress was analyzed by tracking the cell-to-cell transfer of Dendra2, a green-to-red photoconvertible fluorescent protein. In normal condition, the red fluorescence of photoconverted Dendra2 transferred into the adjacent cell via the septal pore with the ratio of 75% in wild type. Upon cold stress at 4oC, translocation ratio of Dendra2 was decreased to 6% in wild type, while Dendra2 still transferred in ΔglpA and ΔAohex1 with the ratios of 45% and 33%, respectively. These results indicated that the regulation of septal pore function was abnormal in ΔglpA.

As gelsolin is generally known as actin-severing protein, actin dynamics in ΔglpA was observed by visualizing with Lifeact-EGFP. While actin predominantly localized at hyphal tip and sub-apical collar in wild type, multiple actin cables and larger sized actin patches were found in ΔglpA. Contractile actin ring typically seen during septum formation was abnormal in ΔglpA with improper actin ring assembly, failure of ring constriction and irregularly orientated constriction.

By fluorescence microscopic observation using EGFP fusion, GlpA was found to localize at hyphal tip as a crescent-like structure. GlpA localized at septum formation site similarly to contractile actin ring, and accumulated at the septal pore with 50% frequency upon hyphal wounding. N-terminal region consisting of 329 amino acids was sufficient for localization at septum formation site. In contrast, C-terminal region containing three gelsolin domains was required for GlpA localization at hyphal tip. The role of gelsolin domains in regulating actin dynamics was evaluated by Lifeact-EGFP in the strain expressing truncated GlpA. The absence of three gelsolin domains resulted in overaccumulation of actin at the hyphal tip as well as abnormal contractile actin ring during septum formation. Truncation of the N-terminal 329 aa led to infrequent septum formation and reduced the ability to plug the septal pore upon hyphal wounding similarly to ΔglpA.

Taken together, I elucidated a novel actin modulating component, which specifically participates in septum formation by regulating actin ring assembly and constriction as well as has a role in septal pore function in Pezizomycotina-specific multicellular fungi.

Chapter 2: Genomic comparison and localization-based screening for identification of novel septum-localizing proteins
Cell-to-cell communication via the septal pore is the fundamental morphological signature of multicellularity in Pezizomycotina. Septal pore is highly dynamic, and Woronin body is the known key regulator. Genomic comparison between genetically characterized unicellular and multicellular fungi could be the strong strategy for finding new components regulating septum formation/septal pore function. Together with collaborators Prof. Nakamura and Dr. Cao from Toyo University, I performed BLAST-based comparison to get genes related to multicellular organization. I searched for conserved genes in multicellular ascomycetes such as Aspergillus fumigatus and Aspergillus nidulans with e-values less than e-100 . A. oryzae genes conserved in ascomycete yeasts such as Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Candida albicans were excluded with e-values more than e-30 , and thus 2104 genes were selected eventually as multicellularityspecific. Second selection was done using gene ontology (GO) term “no biological data available (ND)” for molecular function, cellular component and biological process. Finally, 776 A. oryzae genes were selected as multicellularity-specific uncharacterized.

For localization analysis, selected proteins were expressed as C-terminal EGFP fusion in A. oryzae. To date,767 proteins were characterized, and various localization patterns were found such as cytoplasmic 37.7% (289 proteins), organelle-like 38.6% (296 proteins), no GFP signal 11.9% (91 proteins), hyphal tip 2.3% (18 proteins), plasma membrane 4.0% (31 proteins) and septum/septal pore 7.8% (60 proteins). Out of the 60 proteins showing the septum-related localization, 14 proteins localized at both sides of the septum, 29 proteins at around the septal pore as ring-like structure, and 4 proteins along the septum. Thirteen proteins found in the cytoplasm/organelle in normal condition accumulated at the septal pore upon hyphal wounding

Chapter 3: Functional analysis of septum-localizing proteins in cell-to-cell communication
For functional analysis, I generated deletion strains for 56 of 60 septum-localizing proteins by replacing the genes with the pyrG selective marker. The septal pore plugging ability of the deletion strains was evaluated by hypotonic shock-induced hyphal tip bursting, and hyphae protected from excessive cytoplasmic loss were counted. Approximately 40% of the deletion strains showed reduced ability to prevent excessive loss of cytoplasm. The lowest ability to prevent excessive cytoplasmic loss was observed in some of deletions with genes encoding proteins to accumulate at the septal pore upon wounding

Chapter 4: Functional characterization of transglutaminase in regulation of fungal multicellularity
In the above-mentioned screening, deletion of the gene AO090023000250 encoding a 697 aa protein with transglutaminase domain showed the lowest ability to prevent excessive cytoplasmic loss among the deletion strains. Transglutaminase is Ca2+ -dependent cross-linking enzyme modulating post-translational modification of proteins and plays important physiological functions such as blood clotting and wound healing. Transglutaminase domain characteristically contains conserved catalytic tried. Amino acid substitutions at the putative catalytic residues of AO090023000250 (Cys417Ala and Asp480Ala) resulted in the deletion-like phenotype with a reduced ability of septal pore plugging, suggesting that catalytic triad in transglutaminase is functionally important for septal pore regulation. In truncation analysis, N-terminal region (1-359 aa) was required for accumulation at the septal pore upon hyphal wounding, while C-terminal region including transglutaminase domain evenly distributed in the cytoplasm. These data suggest that N-terminal region targets the septal pore and that transglutaminase domain could perform catalytic activity for protein cross-linking when plugging the septal pore upon hyphal wounding.

In conclusion, a novel protein GlpA identified as Pezizomycotina-specific by bioinformatics tools has a major role in the septum formation by regulating contractile actin ring and proper septal pore function. Furthermore, genomic comparison along with localization screening allowed finding many novel proteins having a role in fungal cell-to-cell communication. These findings suggest that multicellular fungi have been evolved to acquire machineries for the proper regulation of cell-to-cell connectivity via septal pore.

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