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The association between Hfq and RNase E in long‐term nitrogen‐starved Escherichia coli
Author(s) -
McQuail Josh,
Carpousis Agamem J.,
Wigneshweraraj Sivaramesh
Publication year - 2022
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14782
Subject(s) - degradosome , biology , rnase p , exosome complex , rna , polynucleotide phosphorylase , microbiology and biotechnology , escherichia coli , non coding rna , endoribonuclease , biochemistry , enzyme , purine nucleoside phosphorylase , purine , gene
Under conditions of nutrient adversity, bacteria adjust metabolism to minimize cellular energy usage. This is often achieved by controlling the synthesis and degradation of RNA. In Escherichia coli , RNase E is the central enzyme involved in RNA degradation and serves as a scaffold for the assembly of the multiprotein complex known as the RNA degradosome. The activity of RNase E against specific mRNAs can also be regulated by the action of small RNAs (sRNA). In this case, the ubiquitous bacterial chaperone Hfq bound to sRNAs can interact with the RNA degradosome for the sRNA guided degradation of target RNAs. The RNA degradosome and Hfq have never been visualized together in live bacteria. We now show that in long‐term nitrogen starved E. coli , both RNase E and Hfq co‐localize in a single, large focus. This subcellular assembly, which we refer to as the H‐body, forms by a liquid‐liquid phase separation type mechanism and includes components of the RNA degradosome, namely, the helicase RhlB and the exoribonuclease polynucleotide phosphorylase. The results support the existence of a hitherto unreported subcellular compartmentalization of a process(s) associated with RNA management in stressed bacteria.