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Article: Elucidation of the di-c-glycosylation steps during biosynthesis of the antitumor antibiotic, kidamycin.

Heo, Kyung Taek / Lee, Byeongsan / Jang, Jae-Hyuk / Hong, Young-Soo

Frontiers in bioengineering and biotechnology

2022 Volume 10, Page(s) 985696

Abstract: Kidamycins belong to the pluramycin family of antitumor antibiotics that contain di-C-glycosylated angucycline. Owing to its interesting biological activity, several synthetic derivatives of kidamycins are currently being developed. However, the ... ...

Abstract	Kidamycins belong to the pluramycin family of antitumor antibiotics that contain di-C-glycosylated angucycline. Owing to its interesting biological activity, several synthetic derivatives of kidamycins are currently being developed. However, the synthesis of these complex structural compounds with unusual C-glycosylated residues is difficult. In the kidamycin-producing
Language	English
Publishing date	2022-08-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2719493-0
ISSN	2296-4185
ISSN	2296-4185
DOI	10.3389/fbioe.2022.985696
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Article ; Online: Correction: Protective effect of hygrolansamycin C against corticosterone-induced toxicity and oxidative stress-mediated via autophagy and the MAPK signaling pathway.

Roh, Jongtae / Jang, Jun-Pil / Oh, Taehoon / Kim, Jihong / Lee, Byeongsan / Hong, Young-Soo / Jang, Jae-Hyuk / Ko, Sung-Kyun

Pharmacological reports : PR

2024 Volume 76, Issue 2, Page(s) 435–438

Language	English
Publishing date	2024-04-04
Publishing country	Switzerland
Document type	Published Erratum
ZDB-ID	2186248-5
ISSN	2299-5684 ; 1734-1140
ISSN (online)	2299-5684
ISSN	1734-1140
DOI	10.1007/s43440-024-00591-8
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Article ; Online: Protective effect of hygrolansamycin C against corticosterone-induced toxicity and oxidative stress-mediated via autophagy and the MAPK signaling pathway.

Roh, Jongtae / Jang, Jun-Pil / Oh, Taehoon / Kim, Jihong / Lee, Byeongsan / Hong, Young-Soo / Jang, Jae-Hyuk / Ko, Sung-Kyun

Pharmacological reports : PR

2024 Volume 76, Issue 2, Page(s) 368–378

Abstract: Background: Excessive stress, a major problem in modern societies, affects people of all ages worldwide. Corticosterone is one of the most abundant hormones secreted during stressful conditions and is associated with various dysfunctions in the body. In ...

Abstract	Background: Excessive stress, a major problem in modern societies, affects people of all ages worldwide. Corticosterone is one of the most abundant hormones secreted during stressful conditions and is associated with various dysfunctions in the body. In particular, we aimed to investigate the protective effects of hygrolansamycin C (HYGC) against corticosterone-induced cellular stress, a manifestation of excessive stress prevalent in contemporary societies. Methods: We isolated HYGC from Streptomyces sp. KCB17JA11 and subjected PC12 cells to corticosterone-induced stress. The effects of HYGC were assessed by measuring autophagy and the expression of mitogen-activated protein kinase (MAPK) phosphorylation-related genes. We used established cellular and molecular techniques to analyze protein levels and pathways. Results: HYGC effectively protected cells against corticosterone-induced injury. Specifically, it significantly reduced corticosterone-induced oxidative stress and inhibited the expression of autophagy-related proteins induced by corticosterone, which provided mechanistic insight into the protective effects of HYGC. At the signaling level, HYGC suppressed c-Jun N-terminal kinase and extracellular signal-regulated kinase phosphorylation and p38 activation. Conclusions: HYGC is a promising candidate to counteract corticosterone-induced apoptosis and oxidative stress. Autophagy and MAPK pathway inhibition contribute to the protective effects of HYGC. Our findings highlight the potential of HYGC as a therapeutic agent for stress-related disorders and serve as a stepping stone for further exploration and development of stress management strategies.
MeSH term(s)	Rats ; Animals ; Humans ; Corticosterone/toxicity ; p38 Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Signaling System ; Oxidative Stress ; Signal Transduction ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Apoptosis ; Autophagy
Chemical Substances	Corticosterone (W980KJ009P) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2024-03-18
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2186248-5
ISSN	2299-5684 ; 1734-1140
ISSN (online)	2299-5684
ISSN	1734-1140
DOI	10.1007/s43440-024-00572-x
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Article ; Online: Bifunctional and monofunctional α-neoagarooligosaccharide hydrolases from Streptomyces coelicolor A3(2).

Tsevelkhoroloo, Maral / Dhakshnamoorthy, Vijayalakshmi / Hong, Young-Soo / Lee, Chang-Ro / Hong, Soon-Kwang

Applied microbiology and biotechnology

2023 Volume 107, Issue 12, Page(s) 3997–4008

Abstract: Agar is a galactan and a major component of the red algal cell wall. Agar is metabolized only by specific microorganisms. The final step of the β-agarolytic pathway is mediated by α-neoagarooligosaccharide hydrolase (α-NAOSH), which cleaves neoagarobiose ...

Abstract	Agar is a galactan and a major component of the red algal cell wall. Agar is metabolized only by specific microorganisms. The final step of the β-agarolytic pathway is mediated by α-neoagarooligosaccharide hydrolase (α-NAOSH), which cleaves neoagarobiose to D-galactose and 3,6-anhydro-α-L-galactose. In the present study, two α-NAOSHs, SCO3481 and SCO3479, were identified in Streptomyces coelicolor A3(2). SCO3481 (370 amino acids, 41.12 kDa) and SCO3479 (995 amino acids, 108.8 kDa) catalyzed the hydrolysis of the α-(1,3) glycosidic bonds of neoagarobiose, neoagarotetraose, and neoagarohexaose at the nonreducing ends, releasing 3,6-anhydro-α-L-galactose. Both were intracellular proteins without any signal peptides for secretion. Similar to all α-NAOSHs reported to date, SCO3481 belonged to the glycosyl hydrolase (GH) 117 family and formed dimers. On the other hand, SCO3479 was a large monomeric α-NAOSH belonging to the GH2 family with a β-galactosidase domain. SCO3479 also clearly showed β-galactosidase activity toward lactose and artificial substrates, but SCO3481 did not. The optimum conditions for α-NAOSH were pH 6.0 and 25 °C for SCO3481, and pH 6.0 and 30 °C for SCO3479. Enzymatic activity was enhanced by Co
MeSH term(s)	Streptomyces coelicolor/genetics ; Streptomyces coelicolor/metabolism ; Galactose/chemistry ; Agar/metabolism ; Glycoside Hydrolases/metabolism ; Galactosidases/metabolism ; beta-Galactosidase
Chemical Substances	alpha-neoagarooligosaccharide hydrolase (EC 3.2.1.-) ; Galactose (X2RN3Q8DNE) ; Agar (9002-18-0) ; Glycoside Hydrolases (EC 3.2.1.-) ; Galactosidases (EC 3.2.1.-) ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2023-05-15
Publishing country	Germany
Document type	Journal Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-023-12552-x
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Article: A unique dual acyltransferase system shared in the polyketide chain initiation of kidamycinone and rubiflavinone biosynthesis.

Heo, Kyung Taek / Lee, Byeongsan / Hwang, Gwi Ja / Park, Beomcheol / Jang, Jun-Pil / Hwang, Bang Yeon / Jang, Jae-Hyuk / Hong, Young-Soo

Frontiers in microbiology

2023 Volume 14, Page(s) 1274358

Abstract: The pluramycin family of natural products has diverse substituents at the C2 position, which are closely related to their biological activity. Therefore, it is important to understand the biosynthesis of C2 substituents. In this study, we describe the ... ...

Abstract	The pluramycin family of natural products has diverse substituents at the C2 position, which are closely related to their biological activity. Therefore, it is important to understand the biosynthesis of C2 substituents. In this study, we describe the biosynthesis of C2 moieties in
Language	English
Publishing date	2023-10-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1274358
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Article: LacI-Family Transcriptional Regulator DagR Acts as a Repressor of the Agarolytic Pathway Genes in

Tsevelkhoroloo, Maral / Shim, So Heon / Lee, Chang-Ro / Hong, Soon-Kwang / Hong, Young-Soo

publication RETRACTED

Frontiers in microbiology

2021 Volume 12, Page(s) 658657

Abstract: Actinobacteria utilize various polysaccharides in the soil as carbon source by degrading them via extracellular hydrolytic enzymes. Agarose, a marine algal polysaccharide composed of D-galactose and 3,6-anhydro-L-galactose (AHG), is one of the carbon ... ...

Abstract	Actinobacteria utilize various polysaccharides in the soil as carbon source by degrading them via extracellular hydrolytic enzymes. Agarose, a marine algal polysaccharide composed of D-galactose and 3,6-anhydro-L-galactose (AHG), is one of the carbon sources used by
Language	English
Publishing date	2021-04-06
Publishing country	Switzerland
Document type	Journal Article ; Retracted Publication
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.658657
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Article ; Online: Enzymatic Characterization and Comparison of Two Steroid Hydroxylases CYP154C3-1 and CYP154C3-2 from

Subedi, Pradeep / Kim, Ki-Hwa / Hong, Young-Soo / Lee, Joo-Ho / Oh, Tae-Jin

Journal of microbiology and biotechnology

2021 Volume 31, Issue 3, Page(s) 464–474

Abstract: Bacterial cytochrome P450 (CYP) enzymes are responsible for the hydroxylation of diverse endogenous substances with a heme molecule used as a cofactor. This study characterized two CYP154C3 proteins ... ...

Abstract	Bacterial cytochrome P450 (CYP) enzymes are responsible for the hydroxylation of diverse endogenous substances with a heme molecule used as a cofactor. This study characterized two CYP154C3 proteins from
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Benzene/metabolism ; Catalysis ; Cloning, Molecular ; Cytochrome P-450 Enzyme System/genetics ; Cytochrome P-450 Enzyme System/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Ferredoxins/metabolism ; Hydrogen Peroxide/metabolism ; Hydroxylation ; Kinetics ; NADH, NADPH Oxidoreductases/metabolism ; Oxidation-Reduction ; Phylogeny ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Steroid Hydroxylases/genetics ; Steroid Hydroxylases/metabolism ; Steroids/metabolism ; Streptomyces/enzymology ; Streptomyces/genetics ; Substrate Specificity ; Temperature
Chemical Substances	Bacterial Proteins ; Ferredoxins ; Recombinant Proteins ; Steroids ; putidaredoxin (57087-75-9) ; Cytochrome P-450 Enzyme System (9035-51-2) ; Hydrogen Peroxide (BBX060AN9V) ; Steroid Hydroxylases (EC 1.14.-) ; NADH, NADPH Oxidoreductases (EC 1.6.-) ; putidaredoxin reductase (EC 1.6.4.-) ; Benzene (J64922108F)
Language	English
Publishing date	2021-01-04
Publishing country	Korea (South)
Document type	Comparative Study ; Journal Article
ZDB-ID	2412195-2
ISSN	1738-8872 ; 1017-7825
ISSN (online)	1738-8872
ISSN	1017-7825
DOI	10.4014/jmb.2010.10020
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Article: Construction of an Artificial Biosynthetic Pathway for the Styrylpyrone Compound 11-Methoxy-Bisnoryangonin Produced in Engineered

Heo, Kyung Taek / Lee, Byeongsan / Jang, Jae-Hyuk / Ahn, Jung-Oh / Hong, Young-Soo

Frontiers in microbiology

2021 Volume 12, Page(s) 714335

Abstract: A cDNA clone ( ... ...

Abstract	A cDNA clone (named
Language	English
Publishing date	2021-08-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.714335
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Article ; Online: Optimization of Artificial Curcumin Biosynthesis in E. coli by Randomized 5'-UTR Sequences To Control the Multienzyme Pathway.

Kang, Sun-Young / Heo, Kyung Taek / Hong, Young-Soo

ACS synthetic biology

2018 Volume 7, Issue 9, Page(s) 2054–2062

Abstract: One of the optimization strategies of an artificial biosynthetic metabolic flux with a multienzyme pathway is when the enzyme concentrations are present at the appropriate ratios rather than at their maximum expression. Thus, many recent research efforts ...

Abstract	One of the optimization strategies of an artificial biosynthetic metabolic flux with a multienzyme pathway is when the enzyme concentrations are present at the appropriate ratios rather than at their maximum expression. Thus, many recent research efforts have focused on the development of tools that fine-tune the enzyme expression, and these research efforts have facilitated the search for the optimum balance between pathway expression and cell viability. However, the rational approach has some limitations in finding the most optimized expression ratio in in vivo systems. In our study, we focused on fine-tuning the expression level of a six-enzyme reaction for the artificial biosynthesis of curcumin by screening a library of 5'-untranslational region (UTR) sequence mutants made by a multiplex automatic genome engineering (MAGE) tool. From the screening results, a variant (6M08rv) showed about a 38.2-fold improvement in the production of curcumin compared to the parent strain, in which the calculated expression levels of 4-coumarate:CoA ligase (4CL) and phenyldiketide-CoA synthase (DCS), two of the six enzymes, were much lower than those of the parent strain.
MeSH term(s)	5' Untranslated Regions ; Coenzyme A Ligases/genetics ; Curcumin/chemistry ; Curcumin/metabolism ; Escherichia coli/metabolism ; Ligases/genetics ; Metabolic Engineering/methods ; Methyltransferases/genetics ; Plasmids/genetics ; Plasmids/metabolism
Chemical Substances	5' Untranslated Regions ; Methyltransferases (EC 2.1.1.-) ; caffeate O-methyltransferase (EC 2.1.1.68) ; Ligases (EC 6.-) ; Coenzyme A Ligases (EC 6.2.1.-) ; 4-coumarate-CoA ligase (EC 6.2.1.12) ; Curcumin (IT942ZTH98)
Language	English
Publishing date	2018-09-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2161-5063
ISSN (online)	2161-5063
DOI	10.1021/acssynbio.8b00198
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Article ; Online: Ribosomal S6 kinase 2-forkhead box protein O4 signaling pathway plays an essential role in melanogenesis.

Jeung, Dohyun / Lee, Ga-Eun / Chen, Weidong / Byun, Jiin / Nam, Soo-Bin / Park, You-Min / Lee, Hye Suk / Kang, Han Chang / Lee, Joo Young / Kim, Kwang Dong / Hong, Young-Soo / Lee, Cheol-Jung / Kim, Dae Joon / Cho, Yong-Yeon

Scientific reports

2024 Volume 14, Issue 1, Page(s) 9440

Abstract: Although previous studies have examined the signaling pathway involved in melanogenesis through which ultraviolet (UV) or α-melanocyte-stimulating hormones (α-MSH) stimuli act as key inducers to produce melanin at the stratum basal layer of the epidermis, ...

Abstract	Although previous studies have examined the signaling pathway involved in melanogenesis through which ultraviolet (UV) or α-melanocyte-stimulating hormones (α-MSH) stimuli act as key inducers to produce melanin at the stratum basal layer of the epidermis, the signaling pathway regulating melanogenesis is still controversial. This study reports that α-MSH, not UVA and UVB, acted as a major stimulus of melanogenesis in B16F10 melanoma cells. Signaling pathway analysis using gene knockdown technology and chemical inhibitors, the mitogen-activated protein kinase kinase (MEK)/extracellular signal-regulated kinase (ERK)/p90 ribosomal S6 kinase 2 (RSK2) played an important role in melanogenesis. Unexpectedly, LY294002, a PI3K inhibitor, increased melanogenesis without UV or α-MSH stimulation, suggesting that the PI3K/AKT signaling pathway may not be a major signaling pathway for melanogenesis. Chemical inhibition of the MEKs/ERKs/RSK2 signaling pathway using U0126 or BI-D1870 suppressed melanogenesis by stimulation of UVA or α-MSH stimulation, or both. In particular, the genetic depletion of RSK2 or constitutive active (CA)-RSK2 overexpression showed that RSK2 plays a key role in melanogenesis. Interestingly, forkhead box protein O4 (FOXO4) was phosphorylated by RSK2, resulting in the increase of FOXO4's transactivation activity. Notably, the FOXO4 mutant harboring serine-to-alanine replacement at the phosphorylation sites totally abrogated the transactivation activity and reduced melanin production, indicating that RSK2-mediated FOXO4 activity plays a key role in melanogenesis. Furthermore, kaempferol, a flavonoid inhibiting the RSK2 activity, suppressed melanogenesis. In addition, FOXO4-wt overexpression showed that FOXO4 enhance melanin synthesis. Overall, the RSK2-FOXO4 signaling pathway plays a key role in modulating melanogenesis.
MeSH term(s)	Ribosomal Protein S6 Kinases, 90-kDa/metabolism ; Ribosomal Protein S6 Kinases, 90-kDa/genetics ; Melanins/biosynthesis ; Melanins/metabolism ; Animals ; alpha-MSH/metabolism ; alpha-MSH/pharmacology ; Signal Transduction ; Mice ; Cell Line, Tumor ; Forkhead Transcription Factors/metabolism ; Forkhead Transcription Factors/genetics ; Ultraviolet Rays ; Morpholines/pharmacology ; Chromones/pharmacology ; Nitriles/pharmacology ; Butadienes/pharmacology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Melanoma, Experimental/metabolism ; Melanogenesis ; Pteridines
Chemical Substances	Ribosomal Protein S6 Kinases, 90-kDa (EC 2.7.11.1) ; Melanins ; alpha-MSH (581-05-5) ; Forkhead Transcription Factors ; Morpholines ; BI D1870 ; 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (31M2U1DVID) ; Chromones ; Nitriles ; Butadienes ; U 0126 ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; ribosomal protein S6 kinase, 90kDa, polypeptide 3 (EC 2.7.11.1) ; Pteridines
Language	English
Publishing date	2024-04-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-60165-9
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