Polygalacturonase-inhibiting proteins (PGIPs) are plant cell wall proteins that protect plants from fungal invasion. They interact with endopolygalacturonases secreted by phytopathogenic fungi, inhibit their enzymatic activity, and favor the accumulation of oligogalacturonides, which activate plant defense responses. PGIPs are members of the leucine-rich repeat (LRR) protein family that in plants play crucial roles in development, defense against pathogens, and recognition of beneficial microbes. Here we report the crystal structure at 1.7-Å resolution of a PGIP from Phaseolus vulgaris. The structure is characterized by the presence of two ␤-sheets instead of the single one originally predicted by modeling studies. The structure also reveals a negatively charged surface on the LRR concave face, likely involved in binding polygalacturonases. The structural information on PGIP provides a basis for designing more efficient inhibitors for plant protection.

Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.

The ratio of branching fractions R(D^{*-})≡B(B^{0}→D^{*-}τ^{+}ν_{τ})/B(B^{0}→D^{*-}μ^{+}ν_{μ}) is measured using a data sample of proton-proton collisions collected with the LHCb detector at center-of-mass energies of 7 and 8 TeV, corresponding to an integrated luminosity of 3  fb^{-1}. For the first time, R(D^{*-}) is determined using the τ-lepton decays with three charged pions in the final state. The B^{0}→D^{*-}τ^{+}ν_{τ} yield is normalized to that of the B^{0}→D^{*-}π^{+}π^{-}π^{+} mode, providing a measurement of B(B^{0}→D^{*-}τ^{+}ν_{τ})/B(B^{0}→D^{*-}π^{+}π^{-}π^{+})=1.97±0.13±0.18, where the first uncertainty is statistical and the second systematic. The value of B(B^{0}→D^{*-}τ^{+}ν_{τ})=(1.42±0.094±0.129±0.054)% is obtained, where the third uncertainty is due to the limited knowledge of the branching fraction of the normalization mode. Using the well-measured branching fraction of the B^{0}→D^{*-}μ^{+}ν_{μ} decay, a value of R(D^{*-})=0.291±0.019±0.026±0.013 is established, where the third uncertainty is due to the limited knowledge of the branching fractions of the normalization and B^{0}→D^{*-}μ^{+}ν_{μ} modes. This measurement is in agreement with the standard model prediction and with previous results.

Permanent neonatal diabetes mellitus (PNDM) is a rare disorder usually presenting within 6 months of birth.Although several genes have been linked to this disorder, in almost half the cases documented in Italy, the genetic cause remains unknown. Because the Akita mouse bearing a mutation in the Ins2 gene exhibits PNDM associated with pancreatic β cell apoptosis, we sequenced the human insulin gene in PNDM subjects with unidentified mutations. We discovered 7 heterozygous mutations in 10 unrelated probands. In 8 of these patients, insulin secretion was detectable at diabetes onset, but rapidly declined over time. When these mutant proinsulins were expressed in HEK293 cells, we observed defects in insulin protein folding and secretion. In these experiments, expression of the mutant proinsulins was also associated with increased Grp78 protein expression and XBP1 mRNA splicing, 2 markers of endoplasmic reticulum stress, and with increased apoptosis. Similarly transfected INS-1E insulinoma cells had diminished viability compared with those expressing WT proinsulin. In conclusion, we find that mutations in the insulin gene that promote proinsulin misfolding may cause PNDM.