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Phylogenetic Assessment of Understudied Families in Hymenochaetales (Basidiomycota, Fungi)-Reporting Uncovered Species and Reflecting the Recent Taxonomic Updates in the Republic of Korea
Yoonhee Cho, Dohye Kim, Young Woon Lim
J. Microbiol. 2024;62(6):429-447.   Published online May 16, 2024
DOI: https://doi.org/10.1007/s12275-024-00120-5
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AbstractAbstract
Hymenochaetales Oberw. is an order classified in Basidiomycota of Fungi, and species in this order display notable diversity. They exhibit various fruiting body shapes, including clavarioid, effused-reflexed, and resupinate basidiomes. Few mycorrhizal species have been reported in Hymenochaetales, but wood-decaying species dominate the order. Hymenochaetaceae Imazeki & Toki and Schizoporaceae Jülich are the most species-rich families within Hymenochaetales, and most species in the Republic of Korea belong to these two families. As such, current taxonomic classification and nomenclature are not reflected upon species in the remaining Hymenochaetales families. For this study, a multifaceted morphological and multigenetic marker-based phylogenetic investigation was conducted to, firstly, comprehensively identify understudied Hymenochaetales specimens in Korea and, secondly, reflect the updates on the species classification. Five genetic markers were assessed for the phylogenetic analysis: nuclear small subunit ribosomal DNA (nSSU), internal transcribed spacer (ITS), nuclear large subunit ribosomal DNA (nLSU), RNA polymerase II subunit 2 gene (RPB2), and translation elongation factor 1 gene (TEF1). The results from phylogenetic analysis supported 18 species classified under eight families (excluding Hymenochaetaceae and Schizoporaceae) in Korea. Species formerly placed in Rickenellaceae and Trichaptum sensu lato have been systematically revised based on recent taxonomic reconstructions. In addition, our findings revealed one new species, Rickenella umbelliformis, and identified five formerly nationally unreported species classified under five understudied families. Our findings contribute to a better understanding of Hymenochaetales diversity and highlight the need for continued research.
Research Support, Non-U.S. Gov'ts
Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis
Thinh-Phat Cao , Joong-Su Kim , Mi-Hee Woo , Jin Myung Choi , Youngsoo Jun , Kun Ho Lee , Sung Haeng Lee
J. Microbiol. 2016;54(4):311-321.   Published online April 1, 2016
DOI: https://doi.org/10.1007/s12275-016-6029-4
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AbstractAbstract
2-deoxyribose-5-phosphate aldolase (DERA) is a class I aldolase that catalyzes aldol condensation of two aldehydes in the active site, which is particularly germane in drug manufacture. Structural and biochemical studies have shown that the active site of DERA is typically loosely packed and displays broader substrate specificity despite sharing conserved folding architecture with other aldolases. The most distinctive structural feature of DERA compared to other aldolases is short and flexible C-terminal region. This region is also responsible for substrate recognition. Therefore, substrate tolerance may be related to the C-terminal structural features of DERA. Here, we determined the crystal structures of full length and C-terminal truncated DERA from Streptococcus suis (SsDERA). In common, both contained the typical (α/β)8 TIM-barrel fold of class I aldolases. Surprisingly, C-terminal truncation
result
ing in missing the last α9 and β8 secondary elements, allowed DERA to maintain activity comparable to the fulllength enzyme. Specifically, Arg186 and Ser205 residues at the C-terminus appeared mutually supplemental or less indispensible for substrate phosphate moiety recognition. Our results suggest that DERA might adopt a shorter C-terminal region than conventional aldolases during evolution pathway, resulting in a broader range of substrate tolerance through active site flexibility.

Citations

Citations to this article as recorded by  
  • An aldolase-dependent phloroglucinol degradation pathway in Collinsella sp. zg1085
    Yating Li, Tong Xu, Yanqin Tu, Tong Li, Yifeng Wei, Yan Zhou, Ning-Yi Zhou
    Applied and Environmental Microbiology.2024;[Epub]     CrossRef
  • Synthetic Activity of Recombinant Whole Cell Biocatalysts Containing 2‐Deoxy‐D‐ribose‐5‐phosphate Aldolase from Pectobacterium atrosepticum
    Romina Fernández Varela, Ana Laura Valino, Eman Abdelraheem, Rosario Médici, Melisa Sayé, Claudio A. Pereira, Peter‐Leon Hagedoorn, Ulf Hanefeld, Adolfo Iribarren, Elizabeth Lewkowicz
    ChemBioChem.2022;[Epub]     CrossRef
  • Rational engineering of 2-deoxyribose-5-phosphate aldolases for the biosynthesis of (R)-1,3-butanediol
    Taeho Kim, Peter J. Stogios, Anna N. Khusnutdinova, Kayla Nemr, Tatiana Skarina, Robert Flick, Jeong Chan Joo, Radhakrishnan Mahadevan, Alexei Savchenko, Alexander F. Yakunin
    Journal of Biological Chemistry.2020; 295(2): 597.     CrossRef
  • Sensitization of colorectal cancer to irinotecan therapy by PARP inhibitor rucaparib
    Titto Augustine, Radhashree Maitra, Jinghang Zhang, Jay Nayak, Sanjay Goel
    Investigational New Drugs.2019; 37(5): 948.     CrossRef
  • Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis
    Marianne Schulte, Dušan Petrović, Philipp Neudecker, Rudolf Hartmann, Jörg Pietruszka, Sabine Willbold, Dieter Willbold, Vineet Panwalkar
    ACS Catalysis.2018; 8(5): 3971.     CrossRef
  • 1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
    Marianne Schulte, Matthias Stoldt, Philipp Neudecker, Jӧrg Pietruszka, Dieter Willbold, Vineet Panwalkar
    Biomolecular NMR Assignments.2017; 11(2): 197.     CrossRef
Oceanobacillus manasiensis sp. nov., a Moderately Halophilic Bacterium Isolated from the Salt Lakes of Xinjiang, China
Lei Wang , Wen-Yan Liu , Zhi-Jing Gu , San-Feng Chen , Su-Sheng Yang
J. Microbiol. 2010;48(3):312-317.   Published online June 23, 2010
DOI: https://doi.org/10.1007/s12275-010-0135-5
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AbstractAbstract
Three Gram reaction positive, rod-shaped, moderately motile halophilic bacterial strains, designated YD3-56T, YD16, and YH29, were isolated from the sediments of Manasi and Aiding salt lakes in the Xinjiang region of China, respectively. The strains grew optimally at 30-37°C, pH 8-11, in the presence of 5-10% (w/v) NaCl. Phylogenetic analysis based on 16S rRNA gene sequences revealed that the strains were closely related to members of the genus Oceanobacillus, exhibiting 99.1-99.2% similarity to O. kapialis KCTC 13177T, 99.2-99.3% to O. picturae KCTC 3821T, and 94.2-96% sequence similarity to other described Oceanobacillus species. SDS-PAGE of whole cell proteins preparations demonstrated that the strains exhibited high similarity to each other, but distinguished from O. kapialis KCTC 13177T and O. picturae KCTC 3821T (75%). DNA-DNA hybridization revealed that the similarity between the representative strain YD3-56T and O. kapialis KCTC 13177T was 35.3%, and the similarity between YD3-56T and O. picturae KCTC 3821T was 22.3%. Chemotaxonomic analysis of the strains showed menaquinone-7 was the predominant respiratory quinine. Major cellular fatty acids were anteiso-C15:0 and anteiso-C17:0. The polar lipid pattern for strain YD3-56T predominantly contained phosphatidylcholine, and trace to moderate amounts of phosphatidyl ethanolamine and hydroxy-phosphatidyl ethanolamine. The diamino acid in murein was meso-diaminopimelic acid. The DNA G+C content of the strains was 39.7-40.1 mol%. On the basis of these results, the three strains should be classified as a novel species of the genus Oceanobacillus, for which the name Oceanobacillus manasiensis sp. nov. has been proposed, with the type strain as YD3-56T (=CGMCC 1.9105T =NBRC 105903T).

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