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Journal of Bacteriology, May 2000, p. 2468-2475, Vol. 182, No. 9
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Regions of RNase E Important for 5'-End-Dependent
RNA Cleavage and Autoregulated Synthesis
Xunqing
Jiang,
Alexis
Diwa, and
Joel G.
Belasco*
Skirball Institute of Biomolecular Medicine
and Department of Microbiology, New York University School of
Medicine, New York, New York 10016
Received 17 December 1999/Accepted 18 February 2000
RNase E is an important regulatory enzyme that plays a key role in
RNA processing and degradation in Escherichia coli.
Internal cleavage by this endonuclease is accelerated by the presence
of a monophosphate at the RNA 5' end. Here we show that the preference of E. coli RNase E for 5'-monophosphorylated substrates is
an intrinsic property of the catalytically active amino-terminal half
of the enzyme and does not require the carboxy-terminal region. This
property is shared by the related E. coli ribonuclease CafA (RNase G) and by a cyanobacterial RNase E homolog derived from Synechocystis, indicating that the 5'-end dependence of
RNase E is a general characteristic of members of this ribonuclease family, including those from evolutionarily distant species. Although it is dispensable for 5'-end-dependent RNA cleavage, the
carboxy-terminal half of RNase E significantly enhances the ability of
this ribonuclease to autoregulate its synthesis in E. coli.
Despite similarities in amino acid sequence and substrate specificity,
CafA is unable to replace RNase E in sustaining E. coli
cell growth or in regulating RNase E production, even when overproduced
sixfold relative to wild-type RNase E levels.
*
Corresponding author. Mailing address: Skirball
Institute of Biomolecular Medicine, New York University School of
Medicine, 540 First Avenue, New York, NY 10016. Phone: (212) 263-5409. Fax: (212) 263-8951. E-mail:
belasco{at}saturn.med.nyu.edu.
Journal of Bacteriology, May 2000, p. 2468-2475, Vol. 182, No. 9
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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