Single-particle cryo-EM structures of PNPase in complex with the RNA chaperone Hfq and regulatory RNA
Ontology highlight
ABSTRACT:
SUBMITTER: Ben Luisi
PROVIDER: EMPIAR-12067 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.
Dendooven Tom T Sinha Dhriti D Roeselová Alzbeta A Cameron Todd A TA De Lay Nicholas R NR Luisi Ben F BF Bandyra Katarzyna J KJ
Molecular cell 20210621 14
Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic consequences for gene regulation. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq, and sRNA and show that this comp ...[more]
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