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
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: | https://repository.cshl.edu/id/eprint/35220 |
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