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Updated: Aug 16, 2026
Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo
Published on: October 31, 2014
RNase E cleavage in the 5' leader of a tRNA precursor
Fredrik Söderbom1, Staffan G Svärd, Leif A Kirsebom
1Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, Biomedical Centre, SE-751 24 Uppsala, Sweden.
Abstract:
In this study, we have used various tRNA(Tyr)Su3 precursor (pSu3) derivatives that are processed less efficiently by RNase P to investigate if the 5' leader is a target for RNase E. We present data that suggest that RNase E cleaves the 5' leader of pSu3 both in vivo and in vitro. The site of cleavage in the 5' leader corresponds to the cleavage site for a previously identified endonuclease activity referred to as RNase P2/O. Thus, our findings suggest that RNase P2/O and RNase E activities are of the same origin. These data are in keeping with the suggestion that the structure of the 5' leader influences tRNA expression by affecting tRNA processing and indicate the involvement of RNase E in the regulation of cellular tRNA levels.
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