Biochemistry and Molecular Biophysics Laboratory

생화학 및 분자생물물리 연구실

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생화학 및 분자생물물리 연구실

Biochemistry and Molecular Biophysics Lab(BioCheMP)seeks to elucidate the molecular mechanisms underlying DNA metabolism such as DNA replication, transcription, recombination, DNA repair, and chromatin dynamics using a novel single-molecule imaging technique, 'DNA curtain' as well as biophysicochemical methods.
Since DNA contains genetic information, DNA metabolism is the most essential reaction for sustaining life in all kingdoms of life. The key research topic of my laboratory is DNA damage repair. DNA damage induces modification, loss, or distortion of genetic information, which causes malignant human diseases including cancer. Therefore, studying DNA repair is important for understanding many diseases . We are focusing on nucleotide excision repair (NER) and homologous recombination. In addition, we are interested in chromatin dynamics. Human DNA stays as a compact structure called chromatin inside a nucleus. The basic unit of chromatin is a nucleosome, in which DNA is wrapped around histones. The chromatin has a significant influence on DNA metabolism and is dynamically altered by endogenous and environmental factors. We examine the roles and functions of histone chaperones and chromatin remodelers, which contribute to altering chromatin structures. Furthermore, we are investigating how DNA metabolic reactions occur in the chromatin context.

Major research field

single-molecule imaging, DNA metabolism, DNA damage repair, chromatin dynamics

Desired field of research

telomere, live cell imaging

Research Keywords and Topics

Single-molecule imaging, DNA metabolism, DNA damage repair, chromatin dynamics.

Research Publications
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1. Cho C, Jang JW, Kang Y, Watanabe H, Uchihashi T, Kim SJ, Kato K, Lee JY*, and Song J-J*, Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone. Nature Communications. 2019; 10: 5764-5776.
2. Cheon NY, Kim HY, Yeo J-E, Scharer OD and Lee JY, Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B. Nucleic Acids Research. 2019; 47: 8337-8347.
3. Lee JY, Tsuyoshi T, Qi Z, Steinfeld JB, Redding S, Kwon YH, Gaines WA, Zhao X, Sung P, and Greene EC, Base triplet stepping during DNA strand exchange by the Rad51/RecA family of recombinases.
Science. 2015; 349: 977-981.

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