Studies on the interaction of REST with the cholinergic repressor element-1/neuron restrictive silencer element
- Title
- Studies on the interaction of REST with the cholinergic repressor element-1/neuron restrictive silencer element
- Author
- 채영규
- Issue Date
- 2000-07
- Publisher
- Elsevier
- Citation
- MOLECULAR BRAIN RESEARCH, v. 80, issue. 1, page. 88-98
- Abstract
- 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. [Mol. Cell. Biol. 19 (1999) 6788–6795]. 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.
- URI
- https://www.sciencedirect.com/science/article/pii/S0169328X00001297https://repository.hanyang.ac.kr/handle/20.500.11754/162981
- ISSN
- 0169-328X
- DOI
- 10.1016/S0169-328X(00)00129-7
- Appears in Collections:
- COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > MOLECULAR AND LIFE SCIENCE(분자생명과학과) > Articles
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