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. (c) 2005 Elsevier Ltd. All rights reserved

Published in

Journal of Molecular Biology
2005, volume: 352, number: 1, pages: 22-27
Publisher: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD

Authors' information