Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.
A newfound signaling enzyme that diverged from a protein family ubiquitous in bacteria provides mechanistic insights into how new signaling activity emerges to control distinct cellular function and physiology.
A multidimensional chemical mapping strategy enables confident determination of the structures of non-coding RNAs at 1-nm resolution, including previously intractable riboswitch and human regulon states.
Building on previous work (Chatterjee et al., 2014), the mechanism of coincidence detection in bacterial second messenger signaling across membranes is revealed at a molecular level, providing insight into the regulation of a conserved transmembrane receptor.
The global pathogen Vibrio cholerae monitors environmental polyamines to garner information about numbers of ‘self’ versus ‘other’ in the vicinity, and in response, to remain or disperse from biofilms.