Abstract:
:The diversity of mRNA lifetimes in bacterial cells is difficult to reconcile with the relaxed cleavage site specificity of RNase E, the endonuclease most important for governing mRNA degradation. This enzyme has generally been thought to locate cleavage sites by searching freely in three dimensions. However, our results now show that its access to such sites in 5'-monophosphorylated RNA is hindered by obstacles-such as bound proteins or ribosomes or coaxial small RNA (sRNA) base pairing-that disrupt the path from the 5' end to those sites and prolong mRNA lifetimes. These findings suggest that RNase E searches for cleavage sites by scanning linearly from the 5'-terminal monophosphate along single-stranded regions of RNA and that its progress is impeded by structural discontinuities encountered along the way. This discovery has major implications for gene regulation in bacteria and suggests a general mechanism by which other prokaryotic and eukaryotic regulatory proteins can be controlled.
journal_name
Mol Celljournal_title
Molecular cellauthors
Richards J,Belasco JGdoi
10.1016/j.molcel.2019.01.044subject
Has Abstractpub_date
2019-04-18 00:00:00pages
284-295.e5issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(19)30064-4journal_volume
74pub_type
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