Structural basis for double-stranded RNA processing by Dicer

The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.     

Mammalian DNA polymerase: separation of binding from incorporation of deoxyribonucleoside triphosphates

An assay for the binding of deoxyribonucleoside triphosphate with an enzyme-DNA complex has been developed. This binding requires active enzyme and magnesium ion, takes place equally with native or denatured DNA, and may proceed in the absence of demonstrable DNA synthesis. The binding reaction appears to be specific for deoxyribonucleoside triphosphates, and studies on competition indicate that one active site accommodates the four common triphosphates.     

Specific inhibition of nuclear RNA polymerase II by alpha-amanitin

alpha-Amanitin, a toxic substance from the mushroom Amanita phalloides, is a potent inhibitor of DNA-dependent RNA polymerase II (the nucleoplasmic form) from sea urchin, rat liver, and calf thymus. This compound exerts no effect on the activity of polymerase I (nucleolar form) or polymerase III (also nucleoplasmic). The inhibition is due to a specific interaction with polymerase II or with a complex of DNA and polymerase II.