NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonA super(diss)

We have cloned the ubiquitous form of an octamer-binding, 60-kDa protein (NonO) that appears to be the mammalian equivalent of the Drosophila visual and courtship song behavior protein, no-on-transient A/dissonance (nonA super(diss)). A region unprecedently rich in aromatic amino acids containing tw...

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Bibliographic Details
Published in:Molecular and cellular biology 1993-01, Vol.13 (9), p.5593-5603
Main Authors: Yang, Yih-Sheng, Hanke, J H, Carayannopoulos, L, Craft, C M, Capra, J D, Tucker, P W
Format: Article
Language:English
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Summary:We have cloned the ubiquitous form of an octamer-binding, 60-kDa protein (NonO) that appears to be the mammalian equivalent of the Drosophila visual and courtship song behavior protein, no-on-transient A/dissonance (nonA super(diss)). A region unprecedently rich in aromatic amino acids containing two ribonuclear protein binding motifs is highly conserved between the two proteins. A ubiquitous form of NonO is present in all adult tissues, whereas lymphocytes and retina express unique forms of NonO mRNA. The ubiquitous form contains a potential helix-turn-helix motif followed by a highly charged region but differs from prototypic octamer-binding factors by lacking the POU DNA-binding domain. In addition to its conventional octamer duplex-binding, NonO binds single-stranded DNA and RNA at a site independent of the duplex site.
ISSN:0270-7306