NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss

YS Yang, JH Hanke, L Carayannopoulos… - … and cellular biology, 1993 - Am Soc Microbiol
YS Yang, JH Hanke, L Carayannopoulos, CM Craft, JD Capra, PW Tucker
Molecular and cellular biology, 1993Am Soc Microbiol
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 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 …
Abstract
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 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.
American Society for Microbiology