"DICER processes precursor microRNAs (pre-miRNAs) and long double-stranded RNAs (dsRNAs) into small regulatory RNAs, microRNAs (miRNAs) and small interfering RNAs (siRNAs), which target mRNAs for degradation or translational repression through the RNA-induced silencing complex (RISC)."
"Studies have elucidated key aspects of DICER's cleavage mechanism, including 5′- and 3′-end counting rules that determine cleavage sites around 21-22 nucleotides (nt) from the RNA ends. Structural studies have shown that the 3′-end binds within a conserved pocket in DICER's PAZ domain, whereas the 5′-end interacts with a pocket in DICER's platform domain."
"In human, mouse and fly DICER enzymes, the 3′-end terminal phosphate interacts with a cluster of conserved tyrosines and basic residues. Similarly, plant DICER-like enzymes have a conserved 3′-end docking pocket, highlighted by aligned conserved tyrosines, basic residues, and phenylalanine. These findings suggest that the 3′-end binding pocket is conserved across DICER and DICER-like enzymes."
DICER is an evolutionarily conserved RNase III enzyme central to RNA silencing, a gene regulatory mechanism affecting diverse biological processes. It processes precursor microRNAs and long double-stranded RNAs into microRNAs and small interfering RNAs, which target mRNAs for degradation or translational repression via the RNA-induced silencing complex. This activity enables short-hairpin RNA technology, where synthetic shRNAs are processed into siRNA duplexes mimicking endogenous pathways. Research has identified key aspects of DICER's cleavage mechanism, including 5' and 3' end counting rules determining cleavage sites approximately 21-22 nucleotides from RNA ends. The 3' end binds within a conserved pocket in DICER's PAZ domain, while the 5' end interacts with a pocket in the platform domain. These binding pockets are conserved across DICER and DICER-like enzymes.
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