RT Journal Article SR Electronic T1 The formation and function of focus-like structures of Hfq in long-term nitrogen starved Escherichia coli JF bioRxiv FD Cold Spring Harbor Laboratory SP 2020.01.10.901611 DO 10.1101/2020.01.10.901611 A1 Josh McQuail A1 Amy Switzer A1 Lynn Burchell A1 Sivaramesh Wigneshweraraj YR 2020 UL http://biorxiv.org/content/early/2020/01/11/2020.01.10.901611.abstract AB Hfq is an RNA-binding protein that is common to diverse bacterial lineages and has, amongst many, a key role in RNA metabolism. We reveal that Hfq is required by Escherichia coli to adapt to nitrogen (N) starvation. By using single molecule tracking photoactivated localisation microscopy imaging of individual Hfq molecules in live E. coli cells, we have uncovered an unusual behaviour of Hfq: We demonstrate that Hfq forms a distinct and reversible focus-like structure specifically in long-term N starved E. coli cells. We show that foci formation by Hfq is a constituent process of the adaptive response to N starvation and provide evidence which implies that the Hfq foci, analogous to processing (P) bodies of stressed eukaryotic cells, contribute to the management of cellular resources to allow E. coli cells to optimally adapt to long-term N starvation stress.