Open AccessPreferential Cleavage of Degradative Intermediates of rpsT mRNA by the Escherichia coli RNA Degradosome
Author(s) -
Catherine Spickler,
Victoria S. Stronge,
George A. Mackie
Publication year - 2001
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.183.3.1106-1109.2001
Subject(s) - degradosome , rnase p , biology , rnase ph , exosome complex , rnase h , rna , ribonuclease iii , rnase mrp , cleavage (geology) , messenger rna , biochemistry , oligonucleotide , escherichia coli , microbiology and biotechnology , gene , rna interference , paleontology , fracture (geology)
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.