2016年9月
TRF2 Protein Interacts with Core Histones to Stabilize Chromosome Ends
JOURNAL OF BIOLOGICAL CHEMISTRY
- ,
- ,
- 巻
- 291
- 号
- 39
- 開始ページ
- 20798
- 終了ページ
- 20810
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M116.719021
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Mammalian chromosome ends are protected by a specialized nucleoprotein complex called telomeres. Both shelterin, a telomere-specific multi-protein complex, and higher order telomeric chromatin structures combine to stabilize the chromosome ends. Here, we showed that TRF2, a component of shelterin, binds to core histones to protect chromosome ends from inappropriate DNA damage response and loss of telomeric DNA. The N-terminal Gly/Arg-rich domain (GAR domain) of TRF2 directly binds to the globular domain of core histones. The conserved arginine residues in the GAR domain of TRF2 are required for this interaction. A TRF2 mutant with these arginine residues substituted by alanine lost the ability to protect telomeres and induced rapid telomere shortening caused by the cleavage of a loop structure of the telomeric chromatin. These findings showed a previously unnoticed interaction between the shelterin complex and nucleosomal histones to stabilize the chromosome ends.
- リンク情報
- ID情報
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- DOI : 10.1074/jbc.M116.719021
- ISSN : 0021-9258
- eISSN : 1083-351X
- PubMed ID : 27514743
- Web of Science ID : WOS:000384574800040