Daeyoup Lee
KAIST 생명과학과 · 생화학·유전·분자생물학
다이요프 리 교수의 연구실은 에피제네틱스와 전사 조절 메커니즘을 중심으로, 히스톤 수리화학, 복합체 단백질 상호작용, 그리고 전사 인자와의 상호작용을 통해 유전자 발현 조절의 분자 기전을 규명하고자 합니다. 특히, RNA 중합효소 II의 전사 동역학과 관련된 히스톤 탈아세틸화, SWI/SNF 복합체와 p53의 상호작용, HPV E2 단백질과 CBP의 상호작용 등 전사 조절 네트워크의 핵심 요소들을 다룹니다. 또한, 고차원 유전자 분석을 위한 자동화된 NGS 데이터 처리 툴 개발을 통해 실험 생물학과 생물정보학의 융합 연구도 진행하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
Nucleosomes must be deacetylated behind elongating RNA polymerase II to prevent cryptic initiation of transcription within the coding region. RNA polymerase II signals for deacetylation through the methylation of histone H3 lysine 36 (H3K36), which provides the recruitment signal for the Rpd3S histone deacetylase complex (HDAC). The recognition of methyl H3K36 by Rpd3S requires the chromodomain of its Eaf3 subunit. Paradoxically, Eaf3 is also a subunit of the NuA4 acetyltransferase complex, yet
The SWI/SNF complex is required for the transcription of several genes and has been shown to alter nucleosome structure in an ATP-dependent manner. The tumor suppressor protein p53 displays growth and transformation suppression functions that are frequently lost in mutant p53 proteins detected in various cancers. Using genetic and biochemical approaches, we show that several subunits of the human SWI/SNF complex bind to the tumor suppressor protein p53 in vivo and in vitro. The transactivation f
Phosphoserine incorporation: A general strategy for producing recombinant histones with site-specific serine phosphorylation is developed by engineering phosphoseryl-tRNA synthetase (SepRS) and elongation factor Tu (EF-Tu; see picture). Serine-phosphorylated nucleosomes provide direct evidence for crosstalk between phosphorylation and acetylation in histones.
cAMP response element-binding protein-binding protein (CBP) is a eucaryotic transcriptional co-activator that contains multiple protein-protein interaction domains for association with various transcription factors, components of the basal transcriptional apparatus, and other co-activator proteins. Here, we report that CBP is also a co-activator of the human papillomavirus (HPV) E2 protein, which is a sequence-specific transcription/replication factor. We provide biochemical, genetic, and functi
Octopus-toolkit is a stand-alone application for retrieving and processing large sets of next-generation sequencing (NGS) data with a single step. Octopus-toolkit is an automated set-up-and-analysis pipeline utilizing the Aspera, SRA Toolkit, FastQC, Trimmomatic, HISAT2, STAR, Samtools, and HOMER applications. All the applications are installed on the user's computer when the program starts. Upon the installation, it can automatically retrieve original files of various epigenomic and transcripto
The transcriptional regulation of the human telomerase reverse transcriptase (hTERT) gene is a critical step in transformation and differentiation. Human papillomavirus E2 protein inhibits cell growth in HPV-infected cells and triggers apoptosis in HeLa cells. Because E2 induces cell growth suppression and senescence, we hypothesize that the protein may modulate cellular gene expression related to these processes. In this report, we demonstrate that E2 inhibits the hTERT promoter. The mapping of
p300/CREB-binding protein-associated factor (p/CAF), a transcriptional co-activator, interacts with co-activator p300/CBP and acidic transcription factors. p/CAF mediates transcriptional activation by acetylating nucleosomal histones and cellular factors. Previously we reported that CBP binds to human papillomavirus E2 and activates E2-dependent transcription (Lee, D., Lee, B., Kim, J., Kim, D. W., and Choe, J. (2000) J. Biol. Chem. 275, 7045-7051). Here we show that p/CAF binds to the human pap
BRG-1, a component of the human SWI/SNF complex, either activates or represses cellular promoters by modulating chromatin structure via the formation of a multiple polypeptide complex. Human papillomavirus E7 binds and destabilizes pRb, resulting in the blockage of G(1) arrest in the cell cycle. We show here that the high-risk human papillomavirus E7 protein group binds BRG-1 and modulates repression of the c-fos promoter mediated by this protein. In addition, both wild-type and Rb binding-defec
Cumulative evidence suggests that non-proteolytic functions of the proteasome are involved in transcriptional regulation, mRNA export, and ubiquitin-dependent histone modification and thereby modulate the intracellular levels of regulatory proteins implicated in controlling key cellular functions. To date, the non-proteolytic roles of the proteasome have been mainly investigated in euchromatin; their effects on heterochromatin are largely unknown. Here, using fission yeast as a model, we randoml