Structural highlights
Function
[ILF3_MOUSE] May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity).
Publication Abstract from PubMed
Nuclear factors 90 and 45 (NF90 and NF45) form a protein complex involved in the post-transcriptional control of many genes in vertebrates. NF90 is a member of the dsRNA binding domain (dsRBD) family of proteins. RNA binding partners identified so far include elements in 3' untranslated regions of specific mRNAs and several non-coding RNAs. In NF90, a tandem pair of dsRBDs separated by a natively unstructured segment confers dsRNA binding activity. We determined a crystal structure of the tandem dsRBDs of NF90 in complex with a synthetic dsRNA. This complex shows surprising similarity to the tandem dsRBDs from an adenosine-to-inosine editing enzyme, ADAR2 in complex with a substrate RNA. Residues involved in unusual base-specific recognition in the minor groove of dsRNA are conserved between NF90 and ADAR2. These data suggest that, like ADAR2, underlying sequences in dsRNA may influence how NF90 recognizes its target RNAs.
Nuclear factor 90 uses an ADAR2-like binding mode to recognize specific bases in dsRNA.,Jayachandran U, Grey H, Cook AG Nucleic Acids Res. 2015 Dec 27. pii: gkv1508. PMID:26712564[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jayachandran U, Grey H, Cook AG. Nuclear factor 90 uses an ADAR2-like binding mode to recognize specific bases in dsRNA. Nucleic Acids Res. 2015 Dec 27. pii: gkv1508. PMID:26712564 doi:http://dx.doi.org/10.1093/nar/gkv1508
