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- W3132668052 abstract "RNase E in Escherichia coli is an essential endoribonuclease with important roles in stable RNA maturation, in ribosome quality control and in constitutive and regulated mRNA degradation. The Membrane Targeting Sequence (MTS), which forms an amphipathic α-helix, anchors RNase E on the inner cytoplasmic membrane. The absolute conservation of the MTS among -Proteobacteria suggests an important role for RNase E membrane association in RNA metabolism. To elucidate the cellular function of the membrane association of RNase E, we characterized the rne∆MTS strain expressing cytoplasmic RNase E. The results of this study lead us to propose that RNase E membrane association is necessary for RNase E stability, for functional interactions with membrane-associated regulatory factors and for protecting nascent transcripts in the nucleoid from premature interactions with RNase E. In particular, keeping RNase E to the membrane is critical for the specificity of RNase E in ribosome quality control. Membrane association is a new layer of regulation that can explain how RNase E, an enzyme with little sequence specificity and many substrates, can fulfill both ‘maturase’ and ‘degradase’ functions." @default.
- W3132668052 created "2021-03-01" @default.
- W3132668052 creator A5080248404 @default.
- W3132668052 date "2018-11-12" @default.
- W3132668052 modified "2023-09-27" @default.
- W3132668052 title "RNase E membrane-localization : role in RNA degradation and ribosome biogenesis" @default.
- W3132668052 hasPublicationYear "2018" @default.
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