Yen-Hua Huang
Chung Shan Medical University
Binding sitePrimosomeBiophysicsMolecular biologyHelicaseEnzymeChemistryTetramerAmidohydrolaseHydrolaseDihydropyrimidinaseDihydroorotaseNucleotideEscherichia coliDNABiochemistryProtein Data Bank (RCSB PDB)StereochemistryDNA replicationBiologyDNA-binding protein
27Publications
11H-index
245Citations
Publications 29
Newest
PriB is a primosomal protein required for the replication fork restart in bacteria. Although PriB shares structural similarity with SSB, they bind ssDNA differently. SSB consists of an N-terminal ssDNA-binding/oligomerization domain (SSBn) and a flexible C-terminal protein–protein interaction domain (SSBc). Apparently, the largest difference in structure between PriB and SSB is the lack of SSBc in PriB. In this study, we produced the chimeric PriB-SSBc protein in which Klebsiella pneumoniae PriB...
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#1Hong-Hsiang GuanH-Index: 1
#2Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 5 authors...
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#1Hong-Hsiang GuanH-Index: 1
#2Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 5 authors...
Dihydroorotase (DHOase) is the third enzyme in the de novo biosynthesis pathway for pyrimidine nucleotides, and an attractive target for potential anticancer chemotherapy. By screening plant extracts and performing GC–MS analysis, we identified and characterized that the potent anticancer drug plumbagin (PLU), isolated from the carnivorous plant Nepenthes miranda, was a competitive inhibitor of DHOase. We also solved the complexed crystal structure of yeast DHOase with PLU (PDB entry 7CA1), to d...
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Abstract Background Co-trimoxazole, a sulfonamide antibiotic, is used to treat a variety of infections worldwide, and it remains a common first-line medicine for prophylaxis against Pneumocystis jiroveci pneumonia. However, it can cause severe cutaneous adverse reactions (SCAR), including Stevens-Johnson syndrome (SJS), toxic epidermal necrolysis (TEN), and drug reactions with eosinophilia and systemic symptoms (DRESS). The pathomechanism of co-trimoxazole-induced SCAR remains unclear. Objective...
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#1Hong-Hsiang GuanH-Index: 7
#2Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 5 authors...
Abstract Dihydroorotase (DHOase) is the third enzyme in the de novo biosynthesis pathway of pyrimidine nucleotides and considered an attractive target for potential antimalarial, anticancer, and antipathogen chemotherapy. Whether the FDA-approved clinical drug 5-fluorouracil (5-FU) that is used to target the enzyme thymidylate synthase for anticancer therapy can also bind to DHOase remains unknown. Here, we report the crystal structures of DHOase from Saccharomyces cerevisiae (ScDHOase) complexe...
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#1Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
#2Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
Single-stranded DNA (ssDNA)-binding protein (SSB) is essential for DNA metabolic processes. SSB also binds to many DNA-binding proteins that constitute the SSB interactome. The mechanism through which PriA helicase, an initiator protein in the DNA replication restart process, is stimulated by SSB in Escherichia coli (EcSSB) has been established. However, some Gram-positive bacterial SSBs such as Bacillus subtilis SsbA (a counterpart of EcSSB), Staphylococcus aureus SsbA, SsbB, and SsbC do not ac...
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#1Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
#2Yi Lien (CSMU: Chung Shan Medical University)H-Index: 2
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 5 authors...
Abstract Dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. This enzyme is important in pyrimidine metabolism, and blocking its activity would be detrimental to cell survival. This study investigated the dihydropyrimidinase inhibition by plumbagin isolated from the extract of carnivorous plant Nepenthes miranda (Nm). Plumbagin inhibited dihydropyrimidinase with IC50 value of 58 ± 3 μM. Double reciproca...
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#1Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
#2I-Chen Chen (CSMU: Chung Shan Medical University)H-Index: 1
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 3 authors...
Single-stranded DNA (ssDNA)-binding proteins (SSBs) play an important role in all DNA-dependent cellular processes, such as DNA replication, recombination, repair, and replication restart. The N-terminal domain of SSBs forms an oligonucleotide/oligosaccharide-binding (OB) fold for ssDNA binding. The SSB–dC35 complex structure has revealed how an Escherichia coli SSB (EcSSB) tetramer binds to 65-nucleotide (nt)-long ssDNA, namely, the (SSB)65 binding mode. Knowledge on whether the ssDNA-binding m...
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#1Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
#2En-Shyh Lin (National Taichung University of Science and Technology)H-Index: 3
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 3 authors...
Abstract Single-stranded DNA-binding protein (SSB) is essential to cells as it participates in DNA metabolic processes, such as DNA replication, repair, and recombination. Escherichia coli SSB (EcSSB) tetramer cooperatively binds and wraps ssDNA in two major binding modes. In this study, we report the complex crystal structure of Pseudomonas aeruginosa SSB (PaSSB) with ssDNA dT20 at 2.39 A resolution (PDB entry 6JDG) that revealed a new binding mode, namely, (SSB)3:1. In the (SSB)65 mode reveale...
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#1Yen-Hua Huang (CSMU: Chung Shan Medical University)H-Index: 11
#2Zhi-Jun Ning (CSMU: Chung Shan Medical University)H-Index: 1
Last. Cheng-Yang Huang (CSMU: Chung Shan Medical University)H-Index: 18
view all 3 authors...
Abstract Dihydropyrimidinase (DHPase) catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-β-alanine in the second step of the pyrimidine degradation pathway. Whether 5-fluorouracil (5-FU), the best-known fluoropyrimidine that is used to target the enzyme thymidylate synthase for anticancer therapy, can bind to DHPase remains unknown. In this study, we found that 5-FU can form a stable complex with Pseudomonas aeruginosa DHPase (PaDHPase). The crystal structure of PaDHPase comple...
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