NONO
NONO (non-POU domain containing octamer binding, also known as p54(nrb), NRB54, NMT55, P54NRB, P54 and PPP1R114) is a nuclear DNA- and RNA-binding protein. It takes part in pre-mRNA splicing, transcriptional regulation, DNA repair and paraspeckle formation. Browse Assay Genie's current range of NONO research reagents below, or read on for the biology behind the target.
NONO is a DNA- and RNA-binding protein involved in several nuclear processes. It binds the conventional octamer sequence in double-stranded DNA, and also binds single-stranded DNA and RNA at a site independent of the duplex site. It is involved in pre-mRNA splicing, probably as a heterodimer with SFPQ, and interacts with U5 snRNA. Together with PSPC1 it is required for the formation of nuclear paraspeckles, and the SFPQ-NONO heteromer associated with MATR3 may contribute to nuclear retention of defective RNAs.
The SFPQ-NONO heteromer may also modulate topoisomerase I (TOP1) during DNA unwinding, and may support non-homologous end joining required for double-strand break repair and V(D)J recombination. In vitro, the complex strongly stimulates DNA end joining and cooperates with the Ku70-Ku80 dimer. In transcription, the SFPQ-NONO-NR5A1 complex binds the CYP17 promoter, NONO activates transcription through an enhancer element in intracisternal A particle long terminal repeats, and it represses CLOCK-BMAL1 activity to regulate the circadian clock.
Beyond the nucleus-centred roles, NONO is important for the organisation of GABAergic synapses, acting on synaptic RNAs and gephyrin scaffold structure through the GABRA2 transcript. It recruits TET1 to genomic loci during neuronal differentiation, thereby regulating 5-hydroxymethylcytosine levels. NONO also assembles into the HDP-RNP complex, a platform for IRF3 phosphorylation in the cGAS-STING innate immune response, and promotes this pathway in response to HIV-2 but not HIV-1 capsid p24. A rearrangement of the NONO gene with the transcription factor E3 gene has been observed in papillary renal cell carcinoma, and alternatively spliced transcript variants have been described. HGNC places NONO among protein phosphatase 1 regulatory subunits and RNA binding motif proteins.
NONO and PSPC1 are required for nuclear paraspeckle formation, and NONO contributes to pre-mRNA splicing and nuclear retention of defective RNAs.
The SFPQ-NONO heteromer may support non-homologous end joining and TOP1 function, and NONO regulates transcription at promoters such as CYP17.
NONO shapes GABAergic synapses, recruits TET1 during neuronal differentiation and represses CLOCK-BMAL1 activity in the circadian clock.
NONO assembles into the HDP-RNP complex for cGAS-STING signalling, and its fusion with TFE3 has been observed in papillary renal cell carcinoma.
NONO is a nuclear DNA- and RNA-binding protein. It contributes to pre-mRNA splicing, transcriptional regulation, DNA double-strand break repair and the formation of paraspeckles with PSPC1. It also regulates the circadian clock, GABAergic synapse organisation and cGAS-STING innate immune signalling.
NONO is also known as p54(nrb), NRB54, NMT55, P54NRB, P54 and PPP1R114. The HGNC name is non-POU domain containing octamer binding, previously written non-POU-domain-containing, octamer-binding. Alternatively spliced transcript variants have been described for the gene.
Mouse and rat both have a Nono ortholog, so rodent models are available for study. In humans, a rearrangement between NONO and the transcription factor E3 gene has been observed in papillary renal cell carcinoma. Check the datasheet of any product for its validated reactivity.
Binding partners, paraspeckle components and pathway proteins linked to NONO function in RNA processing, DNA repair and innate immunity.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q15233; product specifications from Assay Genie datasheets.