Studies on the interaction of REST4 with the cholinergic repressor element-1/neuron restrictive silencer element.
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 approximately 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 preceding 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.
Lee
J H
JH
Department of Biochemistry, University of Kentucky, Chandler Medical Center, Lexington 40536-0298, USA.
Shimojo
M
M
Chai
Y G
YG
Hersh
L B
LB
D017398:Alternative Splicing; D000818:Animals; D002478:Cells, Cultured; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D016716:PC12 Cells; D011108:Polymers; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D012097:Repressor Proteins / Q000235:genetics / Q000502:physiology*; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology*; D016335:Zinc Fingers / Q000235:genetics; D000099229:RE1-Silencing Transcription Factor
D004247:DNA; D004268:DNA-Binding Proteins; D011108:Polymers; D012097:Repressor Proteins; D014157:Transcription Factors; D000099229:RE1-Silencing Transcription Factor