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The road to RNase P


In 1989, Sidney Altman and Thomas R. Cech shared the Nobel Prize in Chemistry for their discovery of catalytic properties of RNA.

Cech was studying the splicing of RNA in a unicellular organism called Tetrahymena thermophila. He found that the precursor RNA could splice in vitro in the absence of proteins.

Altman studied ribonuclease P (RNase P), a ribonucleoprotein that is a key enzyme in the biosynthesis of tRNA. RNase P is an RNA processing endonuclease that specifically cleaves precursors of tRNA, releasing 5′ precursor sequences and mature tRNAs. RNase P is involved in processing all species of tRNA and is present in all cells and organelles that carry out tRNA synthesis.

What follows is a personal recollection by Altman of how he came to study this remarkable enzyme.

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Figure 1: The structure of acridine.
Figure 2: Nucleotide sequence of su3+ tRNAITyr showing the sequence changes resulting from different single base substitution mutants.


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Altman, S. The road to RNase P. Nat Struct Mol Biol 7, 827–828 (2000).

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