The specificity of tRNA in protein synthesis depends not only on its recognition of the codon
in the mRNA, but also on its recognition of the correct aminoacyl-tRNA synthetase enzyme …

Developing quantitative models of substrate specificity for RNA processing enzymes is a key
step toward understanding their biology and guiding applications in biotechnology and …

The universally conserved ribonucleoprotein RNase P is involved in the processing of tRNA
precursor transcripts. RNase P consists of one RNA and, depending on its origin, a variable …

Base pairing between the substrate and the ribozyme has previously been shown to be
essential for catalytic activity of most ribozymes, but not for RNase P RNA. By using …

The protein component of ribonuclease P (RNase P) binds to the RNA subunit, forming a
functional ribonucleoprotein complex in vivo and enhancing the affinity of the precursor …

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 …

A number of aminoglycosides have been reported to interact and interfere with the function
of various RNA molecules. Among these are 16S rRNA, the group I intron, and the …

Ribonuclease P (RNase P) is a ribonucleoprotein complex that catalyzes the formation of
the mature 5 'end of tRNA. To investigate the role of the protein component in enhancing the …

The universally conserved endoribonuclease P consists of one RNA subunit and,
depending on its origin, a variable number of protein subunits. RNase P is involved in the …

RNase P and RNase mitochondrial RNA processing (MRP) are ribonucleoproteins (RNPs)
that consist of a catalytic RNA and a varying number of protein cofactors. RNase P is …