Journal
MOLECULAR BRAIN RESEARCH
Volume 80, Issue 1, Pages 88-98Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0169-328X(00)00129-7
Keywords
gene transcription; repressor; DNA binding; deletion analysis; oligomerization; glycosylation; zinc finger
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Funding
- NIA NIH HHS [AG05893] Funding Source: Medline
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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 similar to 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. (C) 2000 Elsevier Science B.V. All rights reserved.
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