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Journal of Bacteriology, February 2001, p. 1106-1109, Vol. 183, No. 3
Department of Biochemistry and Molecular
Biology, University of British Columbia, Vancouver, British
Columbia, Canada V6T 1Z3
Received 16 August 2000/Accepted 8 November 2000
RNase E, the principal RNase capable of initiating mRNA decay,
preferentially attacks 5'-monophosphorylated over
5'-triphosphorylated substrates. Site-specific cleavage in vitro of the
rpsT mRNA by RNase H directed by chimeric 2'-O-methyl
oligonucleotides was employed to create truncated RNAs which are
identical to authentic degradative intermediates. The rates of cleavage
of two such intermediates by RNase E in the RNA degradosome are
significantly faster (2.5- to 8-fold) than that of intact RNA. This
verifies the preference of RNase E for degradative intermediates and
can explain the frequent "all-or-none" behavior of mRNAs during the
decay process.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.3.1106-1109.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Preferential Cleavage of Degradative Intermediates
of rpsT mRNA by the Escherichia coli RNA
Degradosome

and
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, D. H. Copp Bldg., University
of British Columbia, 2146 Health Sciences Mall, Vancouver, BC, Canada
V6T 1Z3. Phone: (604) 822-2792. Fax: (604) 822-5227. E-mail:
gamackie{at}interchange.ubc.ca.
Present address: Département de Biochimie, Université
de Montréal, Montreal, Quebec, Canada.
Present address: Department of Biochemistry, University of
Toronto, Toronto, Ontario, Canada.
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