The acceptor stem in pre-tRNAs determines the cleavage specificity of RNase P.

AUTOR(ES)

Holm, P S

RESUMO

As the result of an unusual RNase P specificity, some special, mature tRNAs have acceptor stems with eight instead of the common seven base pairs. The data from numerous studies suggest that some features in the tRNA domain of pre-tRNAs are important for this behaviour. Here, we show that only five base pairs in the acceptor stem of bacterial histidine tRNAs are required to obtain the changed cleavage site in an unrelated eukaryotic serine tRNA.

Documentos Relacionados

• Efficient cleavage of pre-tRNAs by E. coli RNAse P RNA requires the 2'-hydroxyl of the ribose at the cleavage site.
• The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P.
• Lsm Proteins Are Required for Normal Processing of Pre-tRNAs and Their Efficient Association with La-Homologous Protein Lhp1p
• The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem.
• Substrate recognition by RNase P and by the catalytic M1 RNA: identification of possible contact points in pre-tRNAs.