The Chromatin Remodelling Protein CHD1 Contains a Previously Unrecognised C-Terminal Helical Domain
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- 作者：Biswaranjan Mohanty1 ; 3 ; Stephanie Helder1 ; Ana P.G. Silva1 ; Joel P. Mackay1 ; joel.mackay@sydney.edu.au" class="auth_mail" title="E-mail the corresponding author ; Daniel P. Ryan2 ; daniel.ryan@anu.edu.au" class="auth_mail" title="E-mail the corresponding author
- 关键词：PDB ; protein data bank ; CHD ; chromodomain helicase DNA-binding protein ; ISWI ; imitation switch ; CHCT ; CHD1 helical C-terminal domain ; EMSA ; electrophoretic mobility shift assay ; PNK ; polynucleotide kinase ; HMM ; hidden Markov model ; NOE ; nuclear Overhauser effect ; GSH ; glutathione ; PP1D ; protein phosphatase 1D ; CATH ; class ; architecture ; topology and homology ; BLAST ; basic local alignment search tool ; TBE ; Tris-borate EDTA ; SANT ; Swi3 ; Ada2 ; N-CoR ; TFIIIB ; SLIDE ; SANT-like ISWI domain ; BRK ; BRM a
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：23 October 2016
- 年：2016
- 卷：428
- 期：21
- 页码：4298-4314
- 全文大小：2958 K
文摘
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CHD1 is a conserved chromatin remodelling enzyme important for transcription.
An NMR structure of an unrecognised helical domain (CHCT) in CHD1 is reported.
The CHCT domain can bind DNA and nucleosomes.
The CHCT domain is also found in the uncharacterised C17orf64 proteins.
These results enhance our structural understanding of CHD1 enzymes.