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Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P - Nature Communications

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Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P - Nature Communications

Binding of precursor tRNAs (ptRNAs) by bacterial ribonuclease P (RNase P) involves an encounter complex (ES) that isomerizes to a catalytic conformation (ES). However, the structures of intermediates and the conformational changes that occur during binding are poorly understood. Here, we show that pairing between the 5′ leader and 3′RCCA extending the acceptor stem of ptRNA inhibits ES formation.

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Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P - Nature Communications

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Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P - Nature Communications

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