Mechanisms for flexibility in DNA sequence recognition and VP16-induced complex formation by the Oct-1 POU domain.

Details

Serval ID
serval:BIB_624A1221062F
Type
Article: article from journal or magazin.
Collection
Publications
Title
Mechanisms for flexibility in DNA sequence recognition and VP16-induced complex formation by the Oct-1 POU domain.
Journal
Molecular and Cellular Biology
Author(s)
Cleary M.A., Herr W.
ISSN
0270-7306[print], 0270-7306[linking]
Publication state
Published
Issued date
04/1995
Volume
15
Number
4
Pages
2090-2100
Language
english
Notes
Publication types: Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Abstract
DNA binding by the Oct-1 protein is directed by its POU domain, a bipartite DNA-binding domain made up of a POU-specific (POUS) domain and a POU-homeo (POUH) domain, two helix-turn-helix-containing DNA-binding modules that cooperate in DNA recognition. Although the best-characterized DNA target for Oct-1 binding is the octamer sequence ATGCAAAT, Oct-1 also binds a number of different DNA sequence elements. For example, Oct-1 recognizes a form of the herpes simplex virus VP16-responsive TAATGARAT element, called the (OCTA-)TAATGARAT site, that lacks octamer site similarity. Our studies suggest two mechanisms by which Oct-1 achieves flexible DNA sequence recognition. First, an important arginine found in the Oct-1 POUS domain tolerates substitutions of its base contacts within the octamer site. Second, on the (OCTA-)TAATGARAT site, the POUS domain is located on the side of the POUH domain opposite from where it is located on an octamer site. This flexibility of the Oct-1 POU domain in DNA binding also has an impact on its participation in a multiprotein-DNA complex with VP16. We show that Oct-1 POUS domain residues that contact DNA have different effects on VP16-induced complex formation depending on whether the VP16-responsive element involved has overlapping octamer similarity or not.
Keywords
Amino Acid Sequence, Arginine/genetics, Arginine/metabolism, Base Sequence, Binding Sites, Consensus Sequence, DNA/genetics, DNA/metabolism, DNA-Binding Proteins/metabolism, Herpes Simplex Virus Protein Vmw65/metabolism, Host Cell Factor C1, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Octamer Transcription Factor-1, Promoter Regions, Genetic/genetics, Protein Binding, Structure-Activity Relationship, Transcription Factors/metabolism
Pubmed
Web of science
Create date
24/01/2008 16:36
Last modification date
20/08/2019 15:19
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