The POU domain is a bipartite DNA-binding structure

Sturm, Richard A. and Herr, Winship (1988) The POU domain is a bipartite DNA-binding structure. Nature, 336 6199: 601-604. doi:10.1038/336601a0

Author Sturm, Richard A.
Herr, Winship
Title The POU domain is a bipartite DNA-binding structure
Journal name Nature   Check publisher's open access policy
ISSN 0028-0836
Publication date 1988-12
Sub-type Article (original research)
DOI 10.1038/336601a0
Volume 336
Issue 6199
Start page 601
End page 604
Total pages 4
Place of publication London, United Kingdom
Publisher Nature
Language eng
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. 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 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.
Keyword DNA binding protein
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 244 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Fri, 08 Jul 2011, 10:23:16 EST by System User on behalf of Institute for Molecular Bioscience