The POU domain: a large conserved region in the mammalian pit-1, oct-1, oct-2, and Caenorhabditis elegans unc-86 gene products

Herr, W., Sturm, R. A., Clerc, R. G., Corcoran, L. M., Baltimore, D., Sharp, P. A., Ingraham, H. A., Rosenfeld, M. G., Finney, M., Ruvkun, G. (December 1988) The POU domain: a large conserved region in the mammalian pit-1, oct-1, oct-2, and Caenorhabditis elegans unc-86 gene products. Genes Dev, 2 (12A). pp. 1513-6. ISSN 0890-9369

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URL: http://www.ncbi.nlm.nih.gov/pubmed/3215510
DOI: 10.1101/gad.2.12a.1627

Abstract

The POU domain1 (pronounced 'pow') is a highly charged 155–162-amino-acid (aa) region of sequence similarity contained within three mammalian transcription factors. Pit-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 POL -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 binding3,4. Homoeobox domains contain a helix-turn-helix DNA-binding motif6,7, first identified in bacterial repressers8. The helix-turn-helix region of the POU domain is important for DNA binding3,9 and, in other classes of homoeo-containing proteins, the entire homoeo domain is sufficient for DNA binding10–12; 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: Amino Acid Sequence Animals Caenorhabditis/genetics Comparative Study DNA-Binding Proteins/genetics Genes Humans Molecular Sequence Data *Peptide Fragments/genetics Rats Transcription Factors/genetics
Subjects: organism description > animal > C elegans
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
Depositing User: Gail Sherman
Date: December 1988
Date Deposited: 13 Oct 2017 16:33
Last Modified: 03 Nov 2017 21:04
Related URLs:
URI: http://repository.cshl.edu/id/eprint/35163

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