Binding of the RNA chaperone Hfq to the type IV pilus base is crucial for its function in Synechocystis sp. PCC 6803.

Abstract:

:The bacterial RNA-binding protein Hfq functions in post-transcriptional regulation of gene expression. There is evidence in a range of bacteria for specific subcellular localization of Hfq; however, the mechanism and role of Hfq localization remain unclear. Cyanobacteria harbour a subfamily of Hfq that is structurally conserved but exhibits divergent RNA binding sites. Mutational analysis in the cyanobacterium Synechocystis sp. PCC 6803 revealed that several conserved amino acids on the proximal side of the Hfq hexamer are crucial not only for Hfq-dependent RNA accumulation but also for phototaxis, the latter of which depends on type IV pili. Co-immunoprecipitation and yeast two-hybrid analysis show that the secretion ATPase PilB1 (a component of the type IV pilus base) is an interaction partner of Hfq. Fluorescence microscopy revealed that Hfq is localized to the cytoplasmic membrane in a PilB1-dependent manner. Concomitantly, Hfq-dependent RNA accumulation is abrogated in a ΔpilB1 mutant, indicating that localization to the pilus base via interaction with PilB1 is essential for Hfq function in cyanobacteria.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Schuergers N,Ruppert U,Watanabe S,Nürnberg DJ,Lochnit G,Dienst D,Mullineaux CW,Wilde A

doi

10.1111/mmi.12595

subject

Has Abstract

pub_date

2014-05-01 00:00:00

pages

840-52

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

92

pub_type

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