Byeong Jae Lee

ORCID: 0000-0003-4360-8887
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Selenium in Biological Systems
  • RNA modifications and cancer
  • Trace Elements in Health
  • RNA and protein synthesis mechanisms
  • Antimicrobial Peptides and Activities
  • RNA Research and Splicing
  • Glutathione Transferases and Polymorphisms
  • Redox biology and oxidative stress
  • Metalloenzymes and iron-sulfur proteins
  • Genomics and Chromatin Dynamics
  • Cancer-related molecular mechanisms research
  • Biochemical and Structural Characterization
  • Birth, Development, and Health
  • Neurobiology and Insect Physiology Research
  • Bacterial Genetics and Biotechnology
  • Aquaculture disease management and microbiota
  • Epigenetics and DNA Methylation
  • Mitochondrial Function and Pathology
  • Chemical Synthesis and Analysis
  • MicroRNA in disease regulation
  • Invertebrate Immune Response Mechanisms
  • Genetics, Aging, and Longevity in Model Organisms
  • Polyamine Metabolism and Applications
  • Lipid Membrane Structure and Behavior
  • Fungal and yeast genetics research

Seoul National University
2011-2022

Science Applications International Corporation (United States)
2004

Instituto de Biomedicina y Genética Molecular de Valladolid
2003

Institute of Molecular Biology and Genetics
2003

Laboratory of Molecular Genetics
2003

Sejong University
2000

Yeungnam University
2000

Osaka University
2000

National Cancer Institute
1995-1998

National Institutes of Health
1995-1998

The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4, GPX6 (glutathione peroxidases), DIO1, DIO2, DIO3 (iodothyronine deiodinases), MSRB1 (methionine sulfoxide reductase B1), SEPHS2 (selenophosphate synthetase...

10.1074/jbc.m116.756155 article EN cc-by Journal of Biological Chemistry 2016-09-20

Aging and mechanical overload are prominent risk factors for osteoarthritis (OA), which lead to an imbalance in redox homeostasis. The resulting state of oxidative stress drives the pathological transition chondrocytes during OA development. However, specific molecular pathways involved disrupting chondrocyte homeostasis remain unclear. Here, we show that selenophosphate synthetase 1 (SEPHS1) expression is downregulated human mouse cartilage. SEPHS1 downregulation impairs cellular capacity...

10.1038/s41467-022-28385-7 article EN cc-by Nature Communications 2022-02-09

The intracellular generation of reactive oxygen species, together with the thioredoxin and glutathione systems, is thought to participate in redox signaling mammalian cells. activity dependent on status reductase (TR), which turn a selenocysteine residue. Two TR isozymes (TR2 TR3), addition that previously characterized (TR1), have now been identified humans mice. All three contain residue located penultimate position at carboxyl terminus encoded by UGA codon. species human carcinoma cell...

10.1074/jbc.274.35.24522 article EN cc-by Journal of Biological Chemistry 1999-08-01

Translational reading gaps occur when genetic information encoded in mRNA is not translated during the normal course of protein synthesis. This phenomenon has been observed thus far only prokaryotes and a mechanism for extending frame by circumventing stop codon. Reading frames proteins may also be extended suppression codon mediated suppressor tRNA. The rabbit β-globin read-through protein, known, naturally occurring eukaryotes, was sequenced ion trap mass spectrometry to determine how...

10.1021/bi981042r article EN Biochemistry 1998-07-11

Selenium is essential in mammalian embryonic development. However, adults, selenoprotein levels several organs including liver can be substantially reduced by selenium deficiency without any apparent change phenotype. To address the role of selenoproteins function, mice homozygous for a floxed allele encoding selenocysteine (Sec) tRNA([Ser]Sec) gene were crossed with transgenic carrying Cre recombinase under control albumin promoter that expresses specifically liver. Recombination was nearly...

10.1074/jbc.m310470200 article EN cc-by Journal of Biological Chemistry 2004-02-01

The function of selenoprotein W (Se-W) was investigated by cloning the corresponding cDNA from mouse brain and expressing it in CHO cells H1299 human lung cancer cells. Overexpression Se-W markedly reduced sensitivity both cell lines to H2O2 cytotoxicity. intracellular peroxide concentration transfected lower than that parental absence or presence extracellular H2O2. resistance oxidative stress conferred dependent on glutathione. Expression mutants which selenocysteine-13 cysteine-37...

10.1016/s0014-5793(02)02628-5 article EN FEBS Letters 2002-04-07

Selenocysteine is a rare amino acid in protein that encoded by UGA with the requirement of downstream mRNA stem-loop structure, selenocysteine insertion sequence element. To detect selenoproteins <i>Drosophila</i>, entire genome was analyzed novel program searches for elements, followed selenoprotein gene signature analyses. This computational screen and subsequent metabolic labeling <sup>75</sup>Se characterization expression resulted identification three selenoproteins: selenophosphate...

10.1074/jbc.m100422200 article EN cc-by Journal of Biological Chemistry 2001-08-01

Selenocysteine (Sec) tRNA (tRNA([Ser]Sec)) serves as both the site of Sec biosynthesis and adapter molecule for donation this amino acid to protein. The consequences on selenoprotein overexpressing either wild type or a mutant tRNA([Ser]Sec) lacking modified base, isopentenyladenosine, in its anticodon loop were examined by introducing multiple copies corresponding genes into mouse genome. Overexpression wild-type did not affect synthesis. In contrast, levels numerous selenoproteins...

10.1128/mcb.21.11.3840-3852.2001 article EN Molecular and Cellular Biology 2001-06-01

Mice homozygous for an allele encoding the selenocysteine (Sec) tRNA [Ser]Sec gene (Trsp) flanked by loxP sites were generated. Cre recombinase-dependent removal of Trsp in these mice was lethal to embryos. To investigate role mouse mammary epithelium, we deleted this using transgenic carrying recombinase under control tumor virus (MMTV) long terminal repeat or whey acidic protein promoter. While both promoters target expression MMTV-Cre is also expressed spleen and skin. Sec amounts reduced...

10.1128/mcb.23.5.1477-1488.2003 article EN Molecular and Cellular Biology 2003-02-14

Selenium is a nutritionally essential trace element that important for optimal function of the immune system. It incorporated into selenoproteins as amino acid selenocysteine and it known to inhibit expression some viruses. In this study, we show selenium supplementation 3 days prior exposure tumor necrosis factor α (TNF-α) partially suppresses induction human immunodeficiency virus type 1 (HIV-1) replication in both chronically infected T lymphocytic monocytic cell lines. acute HIV-1...

10.1089/aid.1997.13.1325 article EN AIDS Research and Human Retroviruses 1997-10-10

Novel cationic antimicrobial peptides, named nigrocin 1 and 2, were isolated from the skin of Rana nigromaculata their amino acid sequences determined. These peptides manifested a broad spectrum activity against various microorganisms with different specificity. By primary structural analysis, it was revealed that has high sequence homology brevinin 2 but low any other known peptides. To investigate structure–activity relationship which unique structure, circular dichroism (CD) homonuclear...

10.1016/s0014-5793(01)02956-8 article EN FEBS Letters 2001-10-08

Selenophosphate synthetase (SPS) was initially detected in bacteria and shown to synthesize selenophosphate, the active selenium donor. However, mammals have two SPS paralogues, which are designated SPS1 SPS2. Although it is known that SPS2 catalyses synthesis of function remains largely unclear. To examine role mammals, we generated a Sps1-knockout mouse found systemic deficiency led embryos were clearly underdeveloped by embryonic day (E)8.5 virtually resorbed E14.5. The knockout Sps1...

10.1042/bcj20160393 article EN Biochemical Journal 2016-05-17

The selenocysteine (Sec) tRNA[Ser]Sec population in higher vertebrates consists of two major isoacceptors that differ from each other by a single nucleoside modification the wobble position anticodon (position 34). One isoacceptor contains 5-methylcarboxymethyluridine (mcmU) this position, whereas 5-methylcarboxymethyluridine-2′-O-methylribose (mcmUm). modifications these tRNAs are N6-isopentenyladenosine (i6A), pseudouridine (ψ), and 1-methyladenosine (m1A) at positions 37, 55, 58,...

10.1017/s1355838200000388 article EN RNA 2000-09-01

Although selenophosphate synthetase 1 (SPS1/SelD) is an essential gene in Drosophila, its function has not been determined. To elucidate intracellular role, we targeted the removal of SPS1/SelD mRNA Drosophila SL2 cells using RNA interference technology that led to formation vacuole-like globular structures. Surprisingly, these structures were identified as megamitochondria, and only depolarized mitochondria developed into megamitochondria. The levels l(2)01810 glutamine (GS1) increased by...

10.1074/jbc.m109.026492 article EN cc-by Journal of Biological Chemistry 2009-09-16
Coming Soon ...