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Fine-tuning of intrinsic N-Oct-3 POU domain allostery by regulatory DNA targets.

Abstract：

:The 'POU' (acronym of Pit-1, Oct-1, Unc-86) family of transcription factors share a common DNA-binding domain of approximately 160 residues, comprising so-called 'POUs' and 'POUh' sub-domains connected by a flexible linker. The importance of POU proteins as developmental regulators and tumor-promoting agents is due to linker flexibility, which allows them to adapt to a considerable variety of DNA targets. However, because of this flexibility, it has not been possible to determine the Oct-1/Pit-1 linker structure in crystallographic POU/DNA complexes. We have previously shown that the neuronal POU protein N-Oct-3 linker contains a structured region. Here, we have used a combination of hydrodynamic methods, DNA footprinting experiments, molecular modeling and small angle X-ray scattering to (i) structurally interpret the N-Oct-3-binding site within the HLA DRalpha gene promoter and deduce from this a novel POU domain allosteric conformation and (ii) analyze the molecular mechanisms involved in conformational transitions. We conclude that there might exist a continuum running from free to 'pre-bound' N-Oct-3 POU conformations and that regulatory DNA regions likely select pre-existing conformers, in addition to molding the appropriate DBD structure. Finally, we suggest that a specific pair of glycine residues in the linker might act as a major conformational switch.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Alazard R,Mourey L,Ebel C,Konarev PV,Petoukhov MV,Svergun DI,Erard M

doi

10.1093/nar/gkm453

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

4420-32

issue

13

eissn

0305-1048

issn

1362-4962

pii

gkm453

journal_volume

35

pub_type

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