The bacterial heat shock transcription factor, σ32, maintains proper protein homeostasis only after it is targeted to the inner membrane by the signal recognition particle (SRP), thereby enabling integration of protein folding information from both the cytoplasm and cell membrane.

BepA (formerly YfgC) is an Escherichia coli periplasmic protein consisting of an N-terminal protease domain and a C-terminal tetratricopeptide repeat (TPR) domain. We have previously shown that BepA is a dual functional protein with chaperone-like and proteolytic activities involved in membrane assembly and proteolytic quality control of LptD, a major component of the outer membrane lipopolysaccharide translocon. Intriguingly, BepA can associate with the BAM complex: the β-barrel assembly machinery (BAM) driving integration of β-barrel proteins into the outer membrane. However, the molecular mechanism of BepA function and its association with the BAM complex remains unclear. Here, we determined the crystal structure of the BepA TPR domain, which revealed the presence of two subdomains formed by four TPR motifs. Systematic site-directed in vivo photo-cross-linking was used to map the protein-protein interactions mediated by the BepA TPR domain, showing that this domain interacts both with a substrate and with the BAM complex. Mutational analysis indicated that these interactions are important for the BepA functions. These results suggest that the TPR domain plays critical roles in BepA functions through interactions both with substrates and with the BAM complex. Our findings provide insights into the mechanism of biogenesis and quality control of the outer membrane.

The transverse-field Ising models with random exchange interactions in finite dimensions are investigated by means of a real-space renormalization-group method. The scheme yields the exact values of the critical point and critical exponent ν in one dimension and some previous results in the case of random ferromagnetic interactions are reproduced in two and three dimensions. We apply the scheme to spin glasses in transverse fields in two and three dimensions, which have not been analyzed very extensively. The phase diagrams and the critical exponent ν are obtained, and evidence for the existence of an infinite-randomness fixed point in these models is found.

Heat shock response (HSR) generally plays a major role in sustaining protein homeostasis. In Escherichia coli, the activity and amount of the dedicated transcription factor σ32 transiently increase upon heat shock. The initial induction is followed by chaperone-mediated negative feedback to inactivate and degrade σ32. Previous work reported that signal recognition particle (SRP)-dependent targeting of σ32 to the membrane is essential for feedback control, though how SRP recognizes σ32 remained unknown. Extensive photo- and disulfide cross-linking studies in vivo now reveal that the highly conserved regulatory region of σ32 that lacks a consecutive hydrophobic stretch interacts with the signal peptide-binding site of Ffh (the protein subunit of SRP). Importantly, the σ32–Ffh interaction observed was significantly affected by mutations in this region that compromise the feedback regulation, but not by deleting the DnaK/DnaJ chaperones. Homeostatic regulation of HSR thus requires a novel type of SRP recognition mechanism.

The two- and three-dimensional transverse-field Ising models with ferromagnetic exchange interactions are analyzed by means of the real-space renormalization-group method. The basic strategy is a generalization of a method developed for the one-dimensional case, which exploits the exact invariance of the model under renormalization and is known to give the exact values of the critical point and critical exponent ν. The resulting values of the critical exponent ν in two and three dimensions are in good agreement with those for the classical Ising model in three and four dimensions. To the best of our knowledge, this is the first example in which a real-space renormalization group on (2+1)- and (3+1)-dimensional Bravais lattices yields accurate estimates of the critical exponents.