Studies on the interaction of REST4 with the cholinergic repressor element-1/neuron restrictive silencer element
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- 作者：Lee ; Jeong-Heon ; Shimojo ; Masahito ; Chai ; Young-Gyu ; Hersh ; Louis B.
- 关键词：Neurotransmitters ; modulators ; transporters and receptors ; Gene regulation ; Gene transcription ; Repressor ; DNA binding ; Deletion analysis ; Oligomerization ; Glycosylation ; Zinc finger ; RE-1/NRSE ; repressor element-1/neuron restrictive silencer element ; RES
- 刊名：Molecular Brain Research
- 出版年：2000
- 出版时间：July 14, 2000
- 年：2000
- 卷：80
- 期：1
- 页码：88-98
- 全文大小：1.64 M
文摘
REST4 is a neuron specific truncated form of the transcription factor REST/NRSE derived by alternative splicing. REST4 was previously shown to block the repressor activity of REST/NRSF by forming a hetero-oligomer, Shimojo et al. . A series of deletion mutants have now been used to characterize REST4 in terms of its structure and DNA binding. REST4 was found to be O-glycosylated between between residues 87 and 152. Binding of REST4 to the cholinergic RE-1/NRSE was 
1/10 to 1/20 as strong as full length REST/NRSF. DNA binding was enhanced by deletion of the first 86 residues and was found to require all four of the C-terminal zinc fingers as well as a twelve amino acid sequence preceeding the first of these zinc fingers. REST4 can form homo-oligomers, however only the monomer was found to bind to DNA. REST4 binds to the 3′ sequence of the cholinergic NRSE suggesting an anti-parallel orientation of the protein to the DNA.
1/10 to 1/20 as strong as full length REST/NRSF. DNA binding was enhanced by deletion of the first 86 residues and was found to require all four of the C-terminal zinc fingers as well as a twelve amino acid sequence preceeding the first of these zinc fingers. REST4 can form homo-oligomers, however only the monomer was found to bind to DNA. REST4 binds to the 3′ sequence of the cholinergic NRSE suggesting an anti-parallel orientation of the protein to the DNA.