Journal of Microbiology

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Inferences in microbial structural signatures of acne microbiome and mycobiome: Jubin Kim , Taehun Park , Hye-Jin Kim , Susun An , Woo Jun Sul; J. Microbiol. 2021;59(4):369-375. Published online February 10, 2021; DOI: https://doi.org/10.1007/s12275-021-0647-1

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Acne vulgaris, commonly known as acne, is the most common skin disorder and a multifactorial disease of the sebaceous gland. Although the pathophysiology of acne is still unclear, bacterial and fungal factors are known to be involved in. This study aimed to investigate whether the microbiomes and mycobiomes of acne patients are distinct from those of healthy subjects and to identify the structural signatures of microbiomes related to acne vulgaris. A total of 33 Korean female subjects were recruited (Acne group, n = 17; Healthy group, n = 16), and microbiome samples were collected swabbing the forehead and right cheek. To characterize the fungal and bacterial communities, 16S rRNA V4–V5 and ITS1 region, respectively, were sequenced and analysed using Qiime2. There were no significant differences in alpha and beta diversities of microbiomes between the Acne and Healthy groups. In comparison with the ratio of Cutibacterium to Staphylococcus, the acne patients had higher abundance of Staphylococcus compared to Cutibacterium than the healthy individuals. In network analysis with the dominant microorganism amplicon sequence variants (ASV) (Cutibacterium, Staphylococcus, Malassezia globosa, and Malassezia restricta) Cutibacterium acnes was identified to have hostile interactions with Staphylococcus and Malassezia globosa. Accordingly, this
results
suggest an insight into the differences in the skin microbiome and mycobiome between acne patients and healthy controls and provide possible microorganism candidates that modulate the microbiomes associated to acne vulgaris.

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Characterization of Deinococcus radiophilus Thioredoxin Reductase Active with Both NADH and NADPH: Hee-Jeong Seo , Young Nam Lee; J. Microbiol. 2010;48(5):637-643. Published online November 3, 2010; DOI: https://doi.org/10.1007/s12275-010-0283-7

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Abstract: Thioredoxin reductase (TrxR, EC 1.6.4.5) of Deinococcus radiophilus was purified by steps of sonication, ammonium sulfate fractionation, 2'5' ADP Sepharose 4B affinity chromatography, and Sephadex G-100 gel filtration. The purified TrxR, which was active with both NADPH and NADH, gave a 368 U/mg protein of specific activity with 478-fold purification and 18% recovery from the cell-free extract. An isoelectric point of the purified enzymes was ca. 4.5. The molecular weights of the purified TrxR estimated by PAGE and gel filtration were about 63.1 and 72.2 kDa, respectively. The molecular mass of a TrxR subunit is 37 kDa. This suggests that TrxR definitely belongs to low molecular weight TrxR (L-TrxR). The Km and Vmax of TrxR for NADPH are 12.5 μM and 25 μM/min, whereas those for NADH are 30.2 μM and 192 μ M/min. The Km and Vmax for 5, 5'-dithio-bis-2-nitrobenzoic acid (DTNB, a substituted substrate for thioredoxin) are 463 μM and 756 μM/min, respectively. The presence of FAD in TrxR was confirmed with the absorbance peaks at 385 and 460 nm. The purified TrxR was quite stable from pH 3 to 9, and was thermo-stable up to 70°C. TrxR activity was drastically reduced (ca. 70%) by Cu2+, Zn2+, Hg2+, and Cd2+, but moderately reduced (ca. 50%) by Ag+. A significant inhibition of TrxR by N ethylmaleimide suggests an occurrence of cysteine at its active sites. Amino acid sequences at the N-terminus of purified TrxR are H2N-Ser-Glu-Gln-Ala-Gln-Met-Tyr-Asp-Val-Ile-Ile-Val-Gly-Gly-Gly-Pro-Ala-Gly-Leu-Thr-Ala-COOH. These sequences show high similarity with TrxRs reported in Archaea, such as Methanosarcina mazei, Archaeoglobus fulgidus etc.

Purification and Characterization of an Intracellular NADH: Quinone Reductase from Trametes versicolor: Sang-Soo Lee , Dong-Soo Moon , Hyoung T. Choi , Hong-Gyu Song; J. Microbiol. 2007;45(4):333-338.; DOI: https://doi.org/2564 [pii]

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Abstract: Intracellular NADH:quinone reductase involved in degradation of aromatic compounds including lignin was purified and characterized from white rot fungus Trametes versicolor. The activity of quinone reductase was maximal after 3 days of incubation in fungal culture, and the enzyme was purified to homogeneity using ion-exchange, hydrophobic interaction, and gel filtration chromatographies. The purified enzyme has a molecular mass of 41 kDa as determined by SDS-PAGE, and exhibits a broad temperature optimum between 20-40°C, with a pH optimum of 6.0. The enzyme preferred FAD as a cofactor and NADH rather than NADPH as an electron donor. Among quinone compounds tested as substrate, menadione showed the highest enzyme activity followed by 1,4-benzoquinone. The enzyme activity was inhibited by CuSO4, HgCl2, MgSO4, MnSO4, AgNO3, dicumarol, KCN, NaN3, and EDTA. Its Km and Vmax with NADH as an electron donor were 23 μM and 101 mM/mg per min, respectively, and showed a high substrate affinity. Purified quinone reductase could reduce 1,4-benzoquinone to hydroquinone, and induction of this enzyme was higher by 1,4-benzoquinone than those of other quinone compounds.

Occurrence of Thioredoxin Reductase in Deinococcus Species, the UV resistant Bacteria: Hee Jeong Seo , Young Nam Lee; J. Microbiol. 2006;44(4):461-465.; DOI: https://doi.org/2404 [pii]

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Abstract: The occurrence of thioredoxin reductase (NAD(P)H: oxidized-thioredoxin reductase, EC 1.6.4.5, TrxR) in five mesophilic species of Deinococcus was investigated by PAGE. Each species possessed a unique TrxR pattern, for example, a single TrxR characterized D. radiopugnans while multiple forms of TrxR occurred in other Deinococcal spp. Most of TrxRs occurring in Deinococcus showed dual cofactor specificity, active with either NADH or NADPH, although the NADPH specific-TrxR was observed in D. radiophilus and D.proteolyticus.

An FMN-containing NADH-quinone reductase from streptomyces sp: Youn, Hong Duk , Lee, Jin Won , Youn, Hwan , Lee, Jeong Kug , Hah, Yung Chil , Kang, Sa Ouk; J. Microbiol. 1996;34(2):206-213.

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Abstract: NADH-quinone reductase was purified 22-fold from the cytosolic fraction of Streptomyces sp. Imsnu-1 to apparent hemogenity, with an overall yield of 9%, by the purification procedure consisting of ammonium, sulfate precipitation and DEAE Sephacryl S-200 and DEAE 5 PW chromatographies. The molecular mass of the enzyme determined by gel filtration chromatography was found to be 110 kDa. SDS-PAGE revealed that the enzyme consists of two sugunits with a molecular mass of 54 kDa. The enzyme contained 1 mol of FMN per subunit as a cofactor. The A_272/A_457 ratio was 6.14 and the molar extinction coefficients were calculated to be 20, 800 and 25, 400M/sup -1/cm/sup -1/ AT 349 AND 457 nm, respectively. The N-terminal sequence of the enzyme contained the highly conserved fingerprint of ADP-binding domain. The enzyme used NADH as an electron donor and various quinones as electron acceptors. Cytochrome c was practically inactive. Air-stable flavin semiquinone was produced by the addition of NADH to the enzyme. Also, naphthosemiquinone was detected in the reaction mixture containing the enzyme.

Respiratory Chain-Linked Components of the Marine Bacterium Vibrio alginolyticus Affect Each Other: Young Jae Kim; J. Microbiol. 2002;40(2):125-128.

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Abstract: The aerobic respiratory chain of Vibrio alginolyticus possesses two different kinds of NADH oxidase systems, i.e., an Na^+ -dependent NADH oxidase system and an Na^+ -independent NADH oxidase system. When deamino-NADH, which is the only substrate for the Na^+ -dependent NADH oxidase system, was used as a substrate, the maximum activities of Na^+ -dependent NADH:quinone oxidoreductase and Na^+ -dependent NADH oxidase were obtained at about 0.06 M and 0.2 M NaCl, respectively. When NADH, which is a substrate for both Na^+ -dependent and Na^+ -independent NADH oxidase systems was used as a substrate, the NADH oxidase activity had a pH optimum at about 8.0. In contrast, when deamino-NADH was used as a substrate, the NADH oxidase activity had a pH optimum at about 9.0. On the other hand, inside-out membrane vesicles prepared from the wild-type bacterium generated only a very small [delta]pH by the NADH oxidase system, whereas inside-out membrane vesicles prepared from Nap1, which is a mutant defective in the Na^+ pump, generated [delta]pH to a considerable extent by the NADH oxidase system. On the basis of the results, it was concluded that the respiratory chain-linked components of V. alginolyticus affect each other.

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