Abstract
The RNA chaperone Hfq is an Sm protein that facilitates base pairing between bacterial small RNAs (sRNAs) and mRNAs involved in stress response and pathogenesis. Hfq possesses an intrinsically disordered C-terminal domain (CTD) that may tune the function of the Sm domain in different organisms. In Escherichia coli, the Hfq CTD increases kinetic competition between sRNAs and recycles Hfq from the sRNA-mRNA duplex. Here, de novo Rosetta modeling and competitive binding experiments show that the acidic tip of the E. coli Hfq CTD transiently binds the basic Sm core residues necessary for RNA annealing. The CTD tip competes against non-specific RNA binding, facilitates dsRNA release, and prevents indiscriminate DNA aggregation, suggesting that this acidic peptide mimics nucleic acid to auto-regulate RNA binding to the Sm ring. The mechanism of CTD auto-inhibition predicts the chaperone function of Hfq in bacterial genera and illuminates how Sm proteins may evolve new functions.
Article and author information
Author details
Funding
National Institute of General Medical Sciences (R01 GM120425-01)
- Sarah A Woodson
National Institute of General Medical Sciences (R01 GM078221)
- Jeffrey J Gray
National Institute of General Medical Sciences (T32 GM008403-25)
- Jeliazko R Jeliazkov
National Institute of General Medical Sciences (T32 GM007231-40)
- Andrew Santiago-Frangos
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Reviewing Editor
- Ben F Luisi, University of Cambridge, United Kingdom
Publication history
- Received: March 22, 2017
- Accepted: August 3, 2017
- Accepted Manuscript published: August 9, 2017 (version 1)
- Version of Record published: September 20, 2017 (version 2)
- Version of Record updated: October 12, 2017 (version 3)
Copyright
© 2017, Santiago-Frangos et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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