• Title/Summary/Keyword: Fungal structure

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First Discovery of Stereostratum corticioides Causing Rust on the Culm of the Bamboo Pseudosasa japonica

  • Su-Hyun Kim;Tae-Jin Choi
    • Research in Plant Disease
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    • v.30 no.1
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    • pp.20-25
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    • 2024
  • A fungus strain Stereostratum corticioides PKVL1, belonging to the family Pucciniaceae that causes rust in plants, was discovered on the sheath of the bamboo Pseudosasa japonica leading to the death of the infected bamboo in the following year. Microscopic observation of the yellow fungal mass revealed teliospores with an oval, one-septate (two-celled) structure. The average length and width of teliospores were 31.83±3.57 ㎛ and 20.74±1.72 ㎛, respectively. The large-subunit ribosomal RNA gene was amplified using the LR0R and LR7 primers, showing that the strain PKVL1 had a similarity of 99.34% to previously reported S. corticioides. In particular, the two Stereostratum strains form a separate cluster among the fungi in the family Pucciniaceae. This is the first report in the Republic of Korea of fungal rust occurring on the culm of bamboo rather than on the leaves.

Structural Investigation and Homology Modeling Studies of Native and Truncated Forms of $\alpha$-Amylases from Sclerotinia sclerotiorum

  • Ben Abdelmalek, Imen;Urdaci, Maria Camino;Ali, Mamdouh Ben;Denayrolles, Muriel;Chaignepain, Stephane;Limam, Ferid;Bejar, Samir;Marzouki, Mohamed Nejib
    • Journal of Microbiology and Biotechnology
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    • v.19 no.11
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    • pp.1306-1318
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    • 2009
  • The filamentous ascomycete Sclerotinia sclerotiorum is well known for its ability to produce a large variety of hydrolytic enzymes. Two $\alpha$-amylases ScAmy54 and ScAmy43 predicted to play an important role in starch degradation were showed to produce specific oligosaccharides essentially maltotriose that have a considerable commercial interest. Primary structure of the two enzymes was established by N-terminal sequencing, MALDI-TOF masse spectrometry and cDNA cloning. The two proteins have the same N-terminal catalytic domain and ScAmy43 derived from ScAmy54 by truncation of 96 amino acids at the carboxyl-terminal region. Data of genomic analysis suggested that the two enzymes originated from the same $\alpha$-amylase gene and that truncation of ScAmy54 to ScAmy43 occurred probably during S. sclerotiorum cultivation. The structural gene of Scamy54 consisted of 9 exons and 8 introns, containing a single 1,500-bp open reading frame encoding 499 amino acids including a signal peptide of 21 residues. ScAmy54 exhibited high amino acid homology with other liquefying fungal $\alpha$-amylases essentially in the four conserved regions and in the putative catalytic triad. A 3D structure model of ScAmy54 and ScAmy43 was built using the 3-D structure of 2guy from A. niger as template. ScAmy54 is composed by three domains A, B, and C, including the well-known $(\beta/\alpha)_8$ barrel motif in domain A, have a typical structure of $\alpha$-amylase family, whereas ScAmy43 contained only tow domains A and B is the first fungal $\alpha$-amylase described until now with the smallest catalytic domain.

Structure-Antifungal Activity Relationships of Cecropin A-Magainin 2 and Cecropin A-Melittin Hybrid Peptides on Pathogenic Fungal Cells

  • Lee, Dong-Gun;Jin, Zhe-Zhu;Shin, Song-Yub;Kang, Joo-Hyun;Hahm, Kyung-Soo;Kim, Kil-Lyong
    • Journal of Microbiology and Biotechnology
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    • v.8 no.6
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    • pp.595-600
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    • 1998
  • In order to investigate a relationship of the structure-antifungal and hemolytic activities between cecropin A(1-8)-magainin 2(1-12) and cecropin A(1-8)-melittin(1-12) hybrid peptides, several analogues with amino acid substitution at positions 10 (Ile) and 16 (Ser) were designed and synthesized. The increase of the hydrophobicity by substituting with Leu, Phe, and Trp at position 16 in cecropin A(1-8)-magainin 2(1-12) did not have a significant effect on antifungal activity but caused a remarkable increase in hemolytic activity. These results indicate that the hydrophobic property at position 16 of cecropin A(1-8)-magainin 2(1-12) is more correlated to hemolytic activity than to antifungal activity. Replacement with Pro at position 10 of cecropin A(1-8)- magainin 2(1-12) and cecropin A(1-8)-melittin (1-12) caused a remarkable decrease in a-helical contents in the 50% TFE solution and induced a reduction in lytic activity against Aspergillus flavus, and Aspergillus fumigatus. These results demonstrate that flexibility at the central hinge region is essential for lytic activity against fungal cells and $\alpha$-helicity of the peptides.

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Phylogenetics and Gene Structure Dynamics of Polygalacturonase Genes in Aspergillus and Neurospora crassa

  • Hong, Jin-Sung;Ryu, Ki-Hyun;Kwon, Soon-Jae;Kim, Jin-Won;Kim, Kwang-Soo;Park, Kyong-Cheul
    • The Plant Pathology Journal
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    • v.29 no.3
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    • pp.234-241
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    • 2013
  • Polygalacturonase (PG) gene is a typical gene family present in eukaryotes. Forty-nine PGs were mined from the genomes of Neurospora crassa and five Aspergillus species. The PGs were classified into 3 clades such as clade 1 for rhamno-PGs, clade 2 for exo-PGs and clade 3 for exo- and endo-PGs, which were further grouped into 13 sub-clades based on the polypeptide sequence similarity. In gene structure analysis, a total of 124 introns were present in 44 genes and five genes lacked introns to give an average of 2.5 introns per gene. Intron phase distribution was 64.5% for phase 0, 21.8% for phase 1, and 13.7% for phase 2, respectively. The introns varied in their sequences and their lengths ranged from 20 bp to 424 bp with an average of 65.9 bp, which is approximately half the size of introns in other fungal genes. There were 29 homologous intron blocks and 26 of those were sub-clade specific. Intron losses were counted in 18 introns in which no obvious phase preference for intron loss was observed. Eighteen introns were placed at novel positions, which is considerably higher than those of plant PGs. In an evolutionary sense both intron loss and gain must have taken place for shaping the current PGs in these fungi. Together with the small intron size, low conservation of homologous intron blocks and higher number of novel introns, PGs of fungal species seem to have recently undergone highly dynamic evolution.

Comparison of the Genomic Structure of the Heat Shock Protein-88(Hsp88) Genes in the Four Entomopathogenic Fungal Strains, Paecilomyces tenuipes Jocheon-1, P. tenuipes, Cordyceps militaris, and C. pruinosa

  • Liu, Ya-Qi;Park, Nam-Sook;Kim, Yong-Gyun;Kim, Keun-Ki;Park, Hyun-Chul;Son, Hong-Joo;Lee, Sang-Mong
    • International Journal of Industrial Entomology and Biomaterials
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    • v.25 no.1
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    • pp.99-110
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    • 2012
  • Comparison on the genomic structure and phylogenetic relationship of the Hsp88 genes from P. tenuipes Jochoen-1, P. tenuipes, C. militaris and C. pruinosa was described. The Hsp88 genes from the three entomopathogenic strains, P. tenuipes Jocheon-1(strain), P. tenuipes(original species), and C. militaris contain the identical genomic structure, namely 5 introns and 6 exons with the length of 13, 62, 32, 1,438, 306, 288 nucleotides encoding 713 amino acid residues, whereas in case of C. pruinosa, it contains 4 introns and 5 exons with the length of 13, 62, 32, 1,744, 288 nucleotides encoding 713 amino acid residues. The genomic DNA length of the Hsp88 genes from P. tenuipes Jocheon-1 and P. tenuipes are both 2,600 nucleotides long in size. The Hsp88 genes from C. militaris and C. pruinosa are 2,582, 2,576 nucleotides long in size, respectively. Hsp88 genes of the P. tenuipes Jochoen-1, P. tenuipes, C. militaris and C. pruinosa also contain the conserved ATP-binding domain. Phylogenetic analysis of the Hsp genes of the four strains tested in this study showed that the fungal Hsp88 is divided into two separate clades, ascomycetes and deutromycete. Within the ascomycetes fungal clade, the P. tenuipes Jochoen-1 and P. tenuipes formed a subgroup, on the other hand, C. militaris and C. pruinosa formed another subgroup. Pair-wise comparison of P. tenuipes Jocheon-1 Hsp88 with those of P. tenuipes, C. militaris and C. pruinosa Hsp88s revealed significant identity in deduced amino acid sequence among these strains. The P. tenuipes Jocheon-1 Hsp88 showed 99% identity with the P. tenuipes, 97% identity with the C. militaris, and 98% identity with the C. pruinosa.

Effects of Substrates on Fiber Digestion Pattern and Fibrolytic Enzyme Production by Neocallimastix frontalis (기질의 종류가 Neocallimastix frontalis에 의한 섬유소 분해양상과 섬유소 분해 효소 생산에 미치는 영향)

  • Sung, H.G.;Lee, Sung.S.;Ha, J.K.
    • Journal of Animal Science and Technology
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    • v.46 no.5
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    • pp.763-772
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    • 2004
  • The patterns of fungal growth and fiber digestion under the microscope, and tile productions of fibrolytic enzyme were studied in an in vitro culture with Neocallimastix frontalis SA when either filter paper or rice straw was provided as sole energy source. Under the microscopic observation, active zoospores attachment, sporangium development and complex rhizoidal system were founded on the surface and at the edge of filter paper. After 7 days of incubation, a reduced fiber mass, a decreased fiber cohesion and a weakened fiber structure by fungal digestion were clearly observed. Similar fungal development was observed with rice straw, but fungal growth and digestion took place mostly on the damaged and exposed portion of rice straw. Although there were some differences in absolute concentration and pattern, the concentration of both cellulase and xylanase increased with incubation time with the higher activity being obtained with filter paper. Their differences were large especially after 48 and 96hr of incubation(P< 0.05). The filter paper was more good inducer of cellulolytic and xylanolytic enzymes compared with complex substrate, rice straw. These findings suggest that the filter paper is the better energy source for N frontalis than the complex substrate, and structural disintegration by physical process is able to help rumen fungal growth on the lignified roughage although anaerobic rumen fungi have mechanical and enzymatic functions for fiber digestion.

Monocerin and Ziganein: Phytotoxins from Pathogenic Fungus Exserohilum monoceras Inu-1

  • Lim, Chi-Hwan
    • Journal of Applied Biological Chemistry
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    • v.42 no.1
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    • pp.45-47
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    • 1999
  • Two phytotoxic compounds were isolated from a culture of Exserohilum monoceras Inu-1, a fungal pathogen of Barnyard grass. The structure was determined by spectroscopic analyses including 2D NMR experiments. During the isolation procedure, the toxic components were monitored by the assay using Italian ryegrass (Lolium multiflorum Lam.), a host plant of the pathogen. The compounds inhibited the root growth of the host plant seedlings at a level of 100 ppm. While no substantial inhibition was observed even at 300 ppm in non-host plant seedlings such as lettuce and tomato.

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Molecular Dynamics Simulation of Enantioselectivity in Metoprolol in complex

  • Jang, Seok-Young;Park, Kyung-Lae
    • Proceedings of the PSK Conference
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    • 2002.10a
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    • pp.356.3-357
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    • 2002
  • Metoprolol (MT) is one kinds of adrenergic beta-blockers. Its (S)-enantiomer is known to be more active than the (R). Recently. the x-ray structure of beta-blocker. (S)-propranolol (a-naphthyl analogue), complexed in a mould fungal cellulase. Cel7A. was reported and the (R)-form did not build any complex. And in our previous study the conformation and stability of MT in carboxymethylated beta-cyclodextrin (BCD) complex was determined by NMR. HPLC, UV and electrophoresis measurement. (omitted)

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Novel Antifungal Diketopiperazine from Marine Fungus Metabolites

  • Byun, Hee-Guk;Kim, Se-Kwon
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2002.10a
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    • pp.175-176
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    • 2002
  • Rice blast, caused by Pyricularia oryzae (P. oryzae), is generally considered to be the most serious fungal disease of rice by its widespread distribution and destructiveness (Manandhar et al., 1998). The pathogenic fungus directly penetrates into the rice plant from a cellular structure called an appressorium that is formed at the tip of the germ tube. And the fungus can attack any aerial part of the rice plant, including seeds, in which the fungus may overwinter for several years. (omitted)

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