The POU domain is a bipartite DNA-binding structure

Sturm, R. A., Herr, W. (December 1988) The POU domain is a bipartite DNA-binding structure. Nature, 336 (6199). pp. 601-4. ISSN 0028-0836

URL: http://www.ncbi.nlm.nih.gov/pubmed/2904656
DOI: 10.1038/336601a0

Abstract

The POU domain (pronounced 'pow') is a highly charged 155-162-amino-acid (aa) region of sequence similarity contained within three mammalian transcription factors. Pt-1 (ref. 2), Oct-1 (ref. 3) and Oct-2 (ref. 4), and the product of the nematode gene unc-86 (ref. 5) which is involved in determining neural cell lineage. This domain consists of two subdomains, a C-terminal homoeo domain and an N-terminal POU-specific region separated by a short nonconserved linker; the sequence relationship shows that the POU homoeo domains form a distinct POU-related family. In the ubiquitous and lymphoid-specific octamer-motif binding proteins Oct-1 and Oct-2, the POU domain is sufficient for sequence-specific DNA binding. Homoeobox domains contain a helix-turn-helix DNA-binding motif, first identified in bacterial repressors. The helix-turn-helix region of the POU domain is important for DNA binding and, in other classes of homoeo-containing proteins, the entire homoeo domain is sufficient for DNA binding; thus the new POU-specific region could be involved in other functions such as protein-protein interactions. Nevertheless, we show here that in fact the POU domain is a novel bipartite DNA-binding structure in which the POU homoeo and POU-specific regions form two subdomains that are both required for DNA binding but are held together by a flexible linker.

Item Type: Paper
Uncontrolled Keywords: Base Sequence DNA/*metabolism Genes, Homeobox Genes, Viral Molecular Sequence Data Mutation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Simian virus 40/genetics Simplexvirus/genetics Transcription Factors/*genetics/metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
organism description > animal > mammal
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Gail Sherman
Date: 8 December 1988
Date Deposited: 14 Sep 2017 20:12
Last Modified: 14 Sep 2017 20:12
Related URLs:
URI: http://repository.cshl.edu/id/eprint/35220

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