Studies on the interaction of REST4 with the cholinergic repressor element-1/neuron restrictive silencer element

Jeong Heon Lee, Masahito Shimojo, Young Gyu Chai, Louis B. Hersh

Research output: Contribution to journalArticle

36 Scopus citations

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. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)88-98
Number of pages11
JournalMolecular Brain Research
Volume80
Issue number1
DOIs
StatePublished - Jul 14 2000

Keywords

  • DNA binding
  • Deletion analysis
  • Gene transcription
  • Glycosylation
  • Oligomerization
  • Repressor
  • Zinc finger

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Studies on the interaction of REST4 with the cholinergic repressor element-1/neuron restrictive silencer element'. Together they form a unique fingerprint.

  • Cite this