Dissecting cellular components of the secretory pathway in filamentous fungi: insights into their application for protein production

Shoji, Jun‐ya; Arioka, Manabu; Kitamoto, Katsuhiko

doi:10.1007/s10529-007-9516-1

Cited by 36 publications

(32 citation statements)

References 52 publications

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“…The BAS4 promoter/signal peptide (see Supplemental Figure 5 online; Mosquera et al, 2009) and P27 promoter/CUT1 signal peptide (Figure 4) mediate outlining of non-BIC-associated IH and minimal BIC localization. Therefore, preferential BIC accumulation might be explained by enhanced expression of effector genes in BICassociated cells, by a specialized effector secretion process in these cells (Shoji et al, 2008) or by some combination of both. Alternatively, 59-mRNA sequences might mediate preferential BIC accumulation.…”

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

“…Since the first hyphae that grow in host cells exhibit typical filamentous growth ( Figure 1E), standard hyphal tip secretion mechanisms (Steinberg, 2007;Shoji et al, 2008) could account for delivery of effector:FPs into apical BICs. Effector:FP continued to accumulate in BICs that have been left behind by growing bulbous IH (Figure 3), raising the possibility that the original apical secretion apparatus was maintained adjacent to the BIC besides the IH cell.…”

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

“…However, we cannot currently eliminate the possibility that effector:FPs are secreted elsewhere and accumulate in BICs through some unknown mechanism. Fluorescent labeling of components of the standard fungal secretion machinery, the spitzenkö rper and polarisome (Steinberg, 2007;Shoji et al, 2008), will begin to answer questions on mechanisms of secretion and BIC accumulation, as well as questions on location and mechanism for secretion of proteins such as BAS4 that do not show preferential BIC localization.…”

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

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Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

et al. 2010

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Knowledge remains limited about how fungal pathogens that colonize living plant cells translocate effector proteins inside host cells to regulate cellular processes and neutralize defense responses. To cause the globally important rice blast disease, specialized invasive hyphae (IH) invade successive living rice (Oryza sativa) cells while enclosed in host-derived extrainvasive hyphal membrane. Using live-cell imaging, we identified a highly localized structure, the biotrophic interfacial complex (BIC), which accumulates fluorescently labeled effectors secreted by IH. In each newly entered rice cell, effectors were first secreted into BICs at the tips of the initially filamentous hyphae in the cell. These tip BICs were left behind beside the first-differentiated bulbous IH cells as the fungus continued to colonize the host cell. Fluorescence recovery after photobleaching experiments showed that the effector protein PWL2 (for prevents pathogenicity toward weeping lovegrass [Eragrostis curvula]) continued to accumulate in BICs after IH were growing elsewhere. PWL2 and BAS1 (for biotrophyassociated secreted protein 1), BIC-localized secreted proteins, were translocated into the rice cytoplasm. By contrast, BAS4, which uniformly outlines the IH, was not translocated into the host cytoplasm. Fluorescent PWL2 and BAS1 proteins that reached the rice cytoplasm moved into uninvaded neighbors, presumably preparing host cells before invasion. We report robust assays for elucidating the molecular mechanisms that underpin effector secretion into BICs, translocation to the rice cytoplasm, and cell-to-cell movement in rice.

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Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

Section: A Novel Interfacial Structure Associated With Rice Blast Dismentioning

confidence: 99%

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Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

et al. 2010

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“…Along with secreted proteins, proteins destined for other cellular locations such as the plasma membrane, vacuole/lysosome or the Golgi complex, are also transported by the endomembrane system (for reviews on the secretory pathway see Spang, 2008;Shoji et al, 2008;Sallese et al, 2009;Hutagalung & Novick., 2011;Conesa et al, 2001).…”

Section: Overview Of Protein Secretionmentioning

confidence: 99%

The cargo and the transport system: secreted proteins and protein secretion in Trichoderma reesei (Hypocrea jecorina)

2012

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Trichoderma reesei (Hypocrea jecorina) is an efficient cell factory for protein production that is exploited by the enzyme industry. Yields of over 100 g secreted protein l "1 from industrial fermentations have been reported. In this review we discuss the spectrum of proteins secreted by T. reesei and the studies carried out on its protein secretion system. The major enzymes secreted by T. reesei under production conditions are those degrading plant polysaccharides, the most dominant ones being the major cellulases, as demonstrated by the 2D gel analysis of the secretome. According to genome analysis, T. reesei has fewer genes encoding enzymes involved in plant biomass degradation compared with other fungi with sequenced genomes. We also discuss other T. reesei secreted enzymes and proteins that have been studied, such as proteases, laccase, tyrosinase and hydrophobins. Investigation of the T. reesei secretion pathway has included molecular characterization of the pathway components functioning at different stages of the secretion process as well as analysis of the stress responses caused by impaired folding or trafficking in the pathway or by expression of heterologous proteins. Studies on the transcriptional regulation of the secretory pathway have revealed similarities, but also interesting differences, with other organisms, such as a different induction mechanism of the unfolded protein response and the repression of genes encoding secreted proteins under secretion stress conditions. IntroductionThe filamentous fungus Trichoderma reesei (Hypocrea jecorina) is used widely in the enzyme industry as a production organism (for reviews see Penttilä et al., 2004;Kubicek et al., 2009). It is primarily used for production of its native cellulolytic and hemicellulolytic enzymes, but also for production of heterologous proteins. In addition, T. reesei has served as an important model organism of fungal lignocellulose degradation. For example, most of the cellulase and hemicellulase enzymes were identified and characterized for the first time at genetic level in T. reesei (e.g. Shoemaker et al., 1983; Penttilä et al., 1986;Teeri et al., 1987), the molecular structures of these enzymes have been solved (e.g. Rouvinen et al., 1990;Divne et al., 1998) and the gene regulation mechanisms controlling the expression of these enzymes have been elucidated (Kubicek et al., 2009;Aro et al., 2005) from T. reesei. All the T. reesei strains used for research or protein production are derived from a single natural isolate. Extensive mutagenesis and screening programs have created a whole pedigree of strains with improved enzyme production properties. The genome of T. reesei was sequenced by the Joint Genome Institute (Martinez et al., 2008); the sequence is about 34 Mbp and it comprises about 9100 predicted gene models. Both the genome size and the gene number are smaller than that observed for other filamentous fungi. This is mostly explained by the fact that T. reesei has very little redundancy in its genome.During the last two dec...

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“…O complexo de golgi foi localizado por microscopia eletrônica e de fluorescência na região apical dos fungos filamentosos Pisolithus tinctorius (Cole et al, 2000) e A. oryzae (Kuratsu et al, 2007), respectivamente. Este acúmulo apical do complexo de golgi é consistente com a presença de RE e evidencia a importância na predominante secreção nas pontas das hifas (Shoji et al, 2008). (Ronen et al, 2007).…”

Section: -Peptídeo Sinal E Via Secretóriaunclassified

Caracterização funcional do gene codificador de uma proteína com peptídeo sinal, masA, de Aspergillus fumigatus

Cocio¹

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El gen MAS1/GAS2, conocido como "Magnaporthe Apressoria Specific", se identificó como altamente expresado durante la formación de la appressorium fito patógena hongo filamentoso Magnaporthe grisea. En Aspergillus fumigatus, hongo saprofito oportunista, se identificó masA gen ortólogo de MAS1/GAS2 como upregulated en un análisis de transcriptómica expuesto a voriconazol y anidulafungina, antifúngicos que afectan la síntesis de ergosterol y la pared celular, respectivamente. En ambos ortólogos tener una estructura en el extremo N-terminal de la proteína llamada región del péptido señal. Durante la caracterización fenotípica y funcional de gen masA de A. fumigatus se determinó en un análisis in silico de la presencia de péptido señal en la región N-terminal de la proteína. En la caracterización fenotípica de una cepa de A. fumigatus masA -deletado ningún cambio estructural de conidióforos y su aspecto macromorfológico no fue identificado. La cepa deletado masA caracterización es resistente a voriconazol y farnesol que inhiben la síntesis de ergosterol y una molécula de detección de quórum, respectivamente. Al evaluar el nivel de expresión génica masA contra diferentes clases de drogas foi observado el gen súper se expresa cuando se produce daño en la pared celular y la membrana del ADN, la síntesis de lípidos y ácidos grasos, y el estrés oxidativo. En la presencia de daños en la pared celular fúngica causada por anidulafungina, proteína MasA se encuentra cerca de en la pared celular la punta de la hifa y, además, era capaz de transferir al medio extracelular de la proteína fusionada a ella, GFP. Por lo tanto, posiblemente, MasA participa en la vía secretora del hongo sobre todo en momentos de estrés como la ruptura de la pared celular. La capacidad de secreción natural de los hongos filamentosos se ha explotado en el contexto industrial durante décadas. Indicando para este fin, una posible aplicabilidad para este péptido señal.

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Dissecting cellular components of the secretory pathway in filamentous fungi: insights into their application for protein production

Cited by 36 publications

References 52 publications

Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

Translocation ofMagnaporthe oryzaeEffectors into Rice Cells and Their Subsequent Cell-to-Cell Movement

The cargo and the transport system: secreted proteins and protein secretion in Trichoderma reesei (Hypocrea jecorina)

Caracterização funcional do gene codificador de uma proteína com peptídeo sinal, masA, de Aspergillus fumigatus

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