Conserved cysteine residues of Oct-2 POU domain confer sensitivity to oxidation but are dispensable for sequence-specific DNA binding

Détails

ID Serval
serval:BIB_BFDE3F13936B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Conserved cysteine residues of Oct-2 POU domain confer sensitivity to oxidation but are dispensable for sequence-specific DNA binding
Périodique
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Auteur(s)
Rigoni Patrick, Xu Licen, Harshman Keith, Schaffner Walter, Arnosti David N.
ISSN
0167-4781
ISSN-L
1879-2634
Statut éditorial
Publié
Date de publication
05/1993
Volume
1173
Numéro
2
Pages
141-146
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
The POU family of proteins, including the Oct-2 transcription factor, is characterized by a highly conserved bipartite DNA binding domain containing a 'POU homeodomain', distantly related to homeodomains of other DNA binding proteins, and a 'POU specific' domain unique to this class of factors. Prompted by the finding that in vitro DNA binding by Oct-2 is reversibly inhibited by oxidation of the protein, we investigated the role of the cysteine residues in the POU domain. All POU homeodomains identified contain a cysteine in the helix 3 region presumed to contact DNA directly; many (including Oct-2) also contain a less-well conserved cysteine residue(s) in the POU specific domain. Replacement of these cysteines with serine residues rendered the DNA binding domain resistant to oxidation but did not appreciably change the binding to a canonical octamer sequence, suggesting that the conserved cysteine residues are not required for sequence-specific DNA contacts, but may be important for another function.
Mots-clé
Amino Acid Sequence, Base Sequence, Conserved Sequence, Cysteine, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/metabolism, Humans, Molecular Sequence Data, Mutation, Octamer Transcription Factor-2, Oxidation-Reduction, Structure-Activity Relationship, Transcription Factors/chemistry, Transcription Factors/metabolism, Biophysics, Genetics, Biochemistry, Structural Biology
Pubmed
Web of science
Création de la notice
24/01/2008 16:33
Dernière modification de la notice
03/03/2018 21:04
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