PMID:11208812

Citation	Spickler, C, Stronge, V and Mackie, GA (2001) Preferential cleavage of degradative intermediates of rpsT mRNA by the Escherichia coli RNA degradosome. J. Bacteriol. 183:1106-9
Abstract	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.
Links	PubMed PMC94981 Online version:10.1128/JB.183.3.1106-1109.2001
Keywords	Endoribonucleases/metabolism; Escherichia coli/enzymology; Models, Genetic; Multienzyme Complexes/metabolism; Oligonucleotides/metabolism; Polyribonucleotide Nucleotidyltransferase/metabolism; RNA Helicases/metabolism; RNA, Bacterial/metabolism; RNA, Messenger/genetics; RNA, Messenger/metabolism
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