A Putative Polyketide Synthase/Peptide Synthetase from<i>Magnaporthe grisea</i>Signals Pathogen Attack to Resistant Rice[W]

Böhnert, Heidi U.; Fudal, Isabelle; Dioh, Waly; Tharreau, Didier; Nottéghem, Jean-Loup; Lebrun, Marc

doi:10.1105/tpc.104.022715

Cited by 312 publications

(262 citation statements)

References 69 publications

(85 reference statements)

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“…The apicomplexan protist Cryptosporidium parvum, which possesses the same unusual pyruvate:NADP ϩ oxidoreductase as Euglena (8), was recently found to encode a polyketide synthase (66), and various groups of dinoflagellates synthesize large and complex polyketides (67). However, polyketides are not specific to eukaryotic groups that possess plastids (or, in the case of Cryptospridium, have secondarily lost plastids), because various fungi also synthesize polyketides and possess polyketide synthases genes (68,69).…”

Section: Trans-2-enoyl-coa Reductasementioning

confidence: 99%

Mitochondrial trans-2-Enoyl-CoA Reductase of Wax Ester Fermentation from Euglena gracilis Defines a New Family of Enzymes Involved in Lipid Synthesis

Hoffmeister¹,

Piotrowski

Nowitzki³

et al. 2005

Journal of Biological Chemistry

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Under anaerobiosis, Euglena gracilis mitochondria perform a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. An important enzyme of this unusual pathway is trans-2-enoyl-CoA reductase (EC 1.3.1.44), which catalyzes reduction of enoyl-CoA to acyl-CoA. Trans-2-enoyl-CoA reductase from Euglena was purified 1700-fold to electrophoretic homogeneity and was active with NADH and NADPH as the electron donor. The active enzyme is a monomer with molecular mass of 44 kDa. The amino acid sequence of tryptic peptides determined by electrospray ionization mass spectrometry were used to clone the corresponding cDNA, which encoded a polypeptide that, when expressed in Escherichia coli and purified by affinity chromatography, possessed trans-2-enoyl-CoA reductase activity close to that of the enzyme purified from Euglena. Trans-2-enoyl-CoA reductase activity is present in mitochondria and the mRNA is expressed under aerobic and anaerobic conditions. Using NADH, the recombinant enzyme accepted crotonyl-CoA (k m ‫؍‬ 68 M) and trans-2-hexenoyl-CoA (k m ‫؍‬ 91 M). In the crotonyl-CoA-dependent reaction, both NADH (k m ‫؍‬ 109 M) or NADPH (k m ‫؍‬ 119 M) were accepted, with 2-3-fold higher specific activities for NADH relative to NADPH. Trans-2-enoyl-CoA reductase homologues were not found among other eukaryotes, but are present as hypothetical reading frames of unknown function in sequenced genomes of many proteobacteria and a few Gram-positive eubacteria, where they occasionally occur next to genes involved in fatty acid and polyketide biosynthesis. Trans-2-enoyl-CoA reductase assigns a biochemical activity, NAD(P)H-dependent acyl-CoA synthesis from enoylCoA, to one member of this gene family of previously unknown function.

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Section: Trans-2-enoyl-coa Reductasementioning

confidence: 99%

Mitochondrial trans-2-Enoyl-CoA Reductase of Wax Ester Fermentation from Euglena gracilis Defines a New Family of Enzymes Involved in Lipid Synthesis

Hoffmeister¹,

Piotrowski

Nowitzki³

et al. 2005

Journal of Biological Chemistry

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“…This contrasts with two predicted NRPS genes and one NRPS-related gene reported in the N. crassa genome sequence. One of the hybrid PKS-NRPS proteins is encoded by the ACE1 gene, which has recently been shown to act as an avirulence gene 35 . The large number, and expression profile, of PKS and NRPS genes in M. grisea is consistent with the requirements of a fungal pathogen in adapting to diverse environments, perturbing host metabolism and ultimately causing plant cell death.…”

Section: Secondary Metabolic Pathways Of M Griseamentioning

confidence: 99%

The genome sequence of the rice blast fungus Magnaporthe grisea

Dean

Talbot

Ebbole

et al. 2005

Nature

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1,502

1,194

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Magnaporthe grisea is the most destructive pathogen of rice worldwide and the principal model organism for elucidating the molecular basis of fungal disease of plants. Here, we report the draft sequence of the M. grisea genome. Analysis of the gene set provides an insight into the adaptations required by a fungus to cause disease. The genome encodes a large and diverse set of secreted proteins, including those defined by unusual carbohydrate-binding domains. This fungus also possesses an expanded family of G-protein-coupled receptors, several new virulence-associated genes and large suites of enzymes involved in secondary metabolism. Consistent with a role in fungal pathogenesis, the expression of several of these genes is upregulated during the early stages of infection-related development. The M. grisea genome has been subject to invasion and proliferation of active transposable elements, reflecting the clonal nature of this fungus imposed by widespread rice cultivation.Outbreaks of rice blast disease are a serious and recurrent problem in all rice-growing regions of the world, and the disease is extremely difficult to control 1,2 . Rice blast, caused by the fungus Magnaporthe grisea, is therefore a significant economic and humanitarian problem. It is estimated that each year enough rice is destroyed by rice blast disease to feed 60 million people 3 . The life cycle of the rice blast fungus is shown in Fig. 1. Infections occur when fungal spores land and attach themselves to leaves using a special adhesive released from the tip of each spore 4 . The germinating spore develops an appressorium-a specialized infection cell-which generates enormous turgor pressure (up to 8 MPa) that ruptures the leaf cuticle, allowing invasion of the underlying leaf tissue 5,6 . Subsequent colonization of the leaf produces disease lesions from which the fungus sporulates and spreads to new plants. When rice blast infects young rice seedlings, whole plants often die, whereas spread of the disease to the stems, nodes or panicle of older plants results in nearly total loss of the rice grain 2 . Different host-limited forms of M. grisea also infect a broad range of grass species including wheat, barley and millet. Recent reports have shown that the fungus has the capacity to infect plant roots 7 .Here we present our preliminary analysis of the draft genome sequence of M. grisea, which has emerged as a model system for understanding plant-microbe interactions because of both its economic significance and genetic tractability 1,2 . Acquisition of the M. grisea genome sequenceThe genome of a rice pathogenic strain of M. grisea, 70-15, was sequenced through a whole-genome shotgun approach. In all, greater than sevenfold sequence coverage was produced, and a summary of the principal genome sequence data is provided in Table 1 and Supplementary Table S1. The draft genome sequence consists of 2,273 sequence contigs longer than 2 kilobases (kb), ordered and orientated within 159 scaffolds. The total length of all sequence contigs is 38.8 mega...

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“…Additionally, fungal genes that are upregulated during biotrophic invasion are highly enriched for genes encoding biotrophy-associated secreted (BAS) proteins (Mosquera et al, 2009). Except for the Avirulence Conferring Enzyme1 gene (Bö hnert et al, 2004), all known blast AVR genes encode small BAS proteins. These include PWL1 from finger millet (Eleusine coracana) isolates and PWL2 from rice isolates, which both function at the host species level by preventing strains that contain them from infecting weeping lovegrass, Eragrostis curvula Sweigard et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

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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A Putative Polyketide Synthase/Peptide Synthetase fromMagnaporthe griseaSignals Pathogen Attack to Resistant Rice[W]

Cited by 312 publications

References 69 publications

Mitochondrial trans-2-Enoyl-CoA Reductase of Wax Ester Fermentation from Euglena gracilis Defines a New Family of Enzymes Involved in Lipid Synthesis

Mitochondrial trans-2-Enoyl-CoA Reductase of Wax Ester Fermentation from Euglena gracilis Defines a New Family of Enzymes Involved in Lipid Synthesis

The genome sequence of the rice blast fungus Magnaporthe grisea

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

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