Segments of the POU domain influence one another's DNA-binding specificity.

Détails

ID Serval
serval:BIB_F2740998AB4C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Segments of the POU domain influence one another's DNA-binding specificity.
Périodique
Molecular and Cellular Biology
Auteur(s)
Aurora R., Herr W.
ISSN
0270-7306[print], 0270-7306[linking]
Statut éditorial
Publié
Date de publication
02/1992
Volume
12
Numéro
2
Pages
455-467
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The ubiquitously expressed mammalian POU-domain protein Oct-1 specifically recognizes two classes of cis-acting regulatory elements that bear little sequence similarity, the octamer motif ATGCAAAT and the TAATGARAT motif. The related pituitary-specific POU protein Pit-1 also recognizes these two motifs but, unlike Oct-1, binds preferentially to the TAATGARAT motif. Yet in our assay, Pit-1 still binds octamer elements better than does the octamer motif-binding protein Oct-3. The POU domain is responsible for recognizing these diverse regulatory sequences through multiple DNA contacts that include the two POU subdomains, the POU-specific region, and the POU homeodomain. The DNA-binding properties of 10 chimeric POU domains, in which different POU-domain segments are derived from either Oct-1 or Pit-1, reveal a high degree of structural plasticity; these hybrid proteins all bind DNA well and frequently bind particular sites better than does either of the parental POU domains. In these chimeric POU domains, the POU-specific A and B boxes and the hypervariable POU linker can influence DNA-binding specificity. The surprising result is that the influence a particular segment has on DNA-binding specificity can be greatly affected by the origin of other segments of the POU domain and the sequence of the binding site. Thus, the broad but selective DNA-binding specificity of Oct-1 is conferred both by multiple DNA contacts and by dynamic interactions within the DNA-bound POU domain.
Mots-clé
Amino Acid Sequence, Base Sequence, Binding Sites, DNA/metabolism, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/genetics, Electrophoresis, Escherichia coli/genetics, Escherichia coli/metabolism, Gene Expression, Host Cell Factor C1, Macromolecular Substances, Molecular Sequence Data, Octamer Transcription Factor-1, Octamer Transcription Factor-3, Plasmids/genetics, Recombinant Fusion Proteins/chemistry, Recombinant Fusion Proteins/genetics, Regulatory Sequences, Nucleic Acid, Transcription Factor Pit-1, Transcription Factors/chemistry, Transcription Factors/genetics
Pubmed
Web of science
Création de la notice
24/01/2008 16:36
Dernière modification de la notice
03/03/2018 22:40
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