A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.
A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.
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DOI:
10.1016/j.molcel.2021.05.032
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发表时间:
2021-07-15
期刊:
影响因子:
16
通讯作者:
Bandyra KJ
中科院分区:
文献类型:
--
作者:
Dendooven T;Sinha D;Roeselová A;Cameron TA;De Lay NR;Luisi BF;Bandyra KJ
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 complex boosts sRNA stability in vitro. Comparison of structures for PNPase in RNA carrier and degradation modes reveals how the RNA is rerouted away from the active site through interactions with Hfq and the KH and S1 domains. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E and could aid RNA presentation to facilitate regulatory actions on target genes. Cryo-EM structures of PNPase in complex with the RNA chaperone Hfq and regulatory RNA Structural insights into regulatory RNA recognition by Hfq and PNPase Model for stabilization of regulatory RNAs and facilitation of their functions The conserved exoribonuclease PNPase contributes to RNA turnover in many organisms, but in bacteria the enzyme can be re-programmed by the RNA chaperone Hfq and regulatory RNA to switch from degradative to chaperoning roles in RNA-mediated gene regulation. Dendooven et al. provide structural insight into the basis for this functional switch and details of the recognition of complex regulatory RNAs by Hfq and PNPase.
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