Trends in Biochemical Sciences
TFIIIA: nine fingers - three hands?
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Cited by (39)
Emerging Epigenetic Regulation of Circular RNAs in Human Cancer
2019, Molecular Therapy Nucleic AcidsCitation Excerpt :They are a special class of noncoding RNAs derived from the back-splicing or exon skipping of pre-mRNAs. Unlike linear RNAs, circRNAs do not have a 5-cap and 3-poly(A) tails, which are produced by back-splicing exons, and the downstream 3-splicing donor is connected in reverse bond to the upstream 5-split acceptor.3 circRNAs are stable due to their special circular structure, and they are not easily degraded by exonucleases, thus having a longer half-life.
Towards understanding the molecular recognition process in prokaryotic zinc-finger domain
2015, European Journal of Medicinal ChemistryCitation Excerpt :Transcription, DNA replication and repair are key dynamic cellular processes that require extremely tight regulation by DNA-binding proteins. Zinc fingers of the Cys2His2 class (or classical), first discovered in Transcription factor IIIA (TFIIIA) [1–3], constitute one of the most abundant and important structural motifs involved in protein-DNA interactions and is also known to be involved in binding of RNA, lipids, and proteins [4–7]. The classical Cys2His2 zinc finger is a small domain that typically contains a repeated 28–30 amino acid sequence in which a zinc ion, crucial for its stability, is tetrahedrally coordinated by two cysteines and two histidine residues.
Identification of differentially expressed genes in haemocytes of the crayfish (Procambarus clarkii) infected with white spot syndrome virus by suppression subtractive hybridization and cDNA microarrays
2009, Fish and Shellfish ImmunologyCitation Excerpt :Zinc-finger proteins are mainly found in DNA-binding proteins such as transcription factors, but some of them (e.g. CCCH and CCHC) also bind to RNA and even participate in protein–protein interactions. One member of the family, transcription factor IIIA (TFIIIA), binds both DNA and RNA [31]. While the binding of zinc-finger proteins to DNA has been well studied, with numerous structures available, the molecular basis of RNA recognition by zinc-finger proteins remained elusive until recently [32].
Domain organization and functional properties of yeast transcription factor IIIA species with different zinc stoichiometries
1999, Journal of Biological ChemistryGenetic analysis of Xenopus transcription factor IIIA
1998, Journal of Molecular Biology