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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2024.12
- 수록면
- 199 - 208 (10page)
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초록· 키워드
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Histones are structural proteins organizing DNA into nucleosomes in chromatin environment. Lysine residues of histone N-terminal have positive charge, facilitating stable interaction with negatively charged DNA in nucleosomes. Each lysine residue can be covalently modified by the addition of acetyl group and removal of it, which is called as histone acetylation and deacetylation. These modifications are catalyzed by histone acetyltransferases and deacetylases, respectively. Histone acetylation weakens interaction between histone and DNA in nucleosomes, increasing the accessibility of nucleosomal DNA to other proteins such as transcription factors and coactivators. In addition, acetylated lysine residues act as recognition points for bromodomain that is present in many kinds of coactivators. Thus, histone acetylation plays essential roles in activating chromatin structure and promoting nuclear events such as gene transcription, DNA replication and DNA repair. The failure of histone acetylation and deacetylation causes serious diseases including cancer. This review explains the basic concept of histone acetylation based on studies in biochemistry and molecular biology fields and may be helpful to understand chromatin structure, histone modifications and epigenetics.
목차
ABSTRACT
서론
히스톤 아세틸화
히스톤 아세틸화효소
히스톤 탈아세틸화효소
히스톤 아세틸화의 역할
히스톤 아세틸화와 암
결론
REFERENCES
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