This paper measured the ecophysiological responses of Populus cathayana Rehd., Salix longistamina C. Wang et P. Y. Fu., and Ulmus pumila L. to high altitude in the Tibetan Plateau based on changes in water relations, gas exchange, and chlorophyll fluorescence. P. cathayana and U. pumila have higher survival rates than S. longistamina, but the latter has highest biomass. S. longistamina has higher water-use efficiency (WUE), lower transpiration rates (E), higher water potential (Ψ), highest light saturation point (LSP) and higher photosystem II (PSII) photochemistry efficiency (F_v’/F_m’) and non-photochemistry quenching (NPQ) than the other species, and is thus adapted to its habitat for afforestation. U. pumila has lower E, light compensation point (LCP), dark respiration (R_d), F_v’/F_m’ and electron transport rate (ETR), with higher Ψ, apparent quantum yield (AQY), net photosynthetic rate (P_n) and non-photochemical quenching (NPQ), which helps it maintain water balance and utilize weak light to survive at high altitude. Relative low WUE, Ψ, R_d, NPQ, with high E, P_n, F_v’/F_m’ and biomass, imply that P. cathayana is more suitable for shelterbelt forests than for a semi-arid habitat. These three species can adapt to high-altitude conditions by different physiological mechanisms and morphological characteristics, which can provide a theoretical basis for afforestation and forest management in the Qinghai Tibetan Plateau.

Uncharacterized protein STY1099, encoded by the yccT gene, was previously identified as the most altered (i.e., upregulated) protein among the ZnO nanoparticle (NP) stimulon of Salmonella enterica serovar Enteritidis. Here we combined various stress response-related assays with functional genetics, global transcriptomic and proteomic analyses to characterize the yccT gene and its STY1099 product. Exposure of S. enterica Enteritidis to H₂O₂ (i.e., hydrogen peroxide) resulted in a significant (p < 0.0001) upregulation of the yccT gene, whereas exposure to paraquat (i.e., superoxide) did not alter the expression of the yccT gene. The ∆yccT mutant of S. enterica Enteritidis exposed to 0.75 mM H₂O₂, showed significantly reduced (p < 0.05) viability compared to the wild type strain. Further, comparative transcriptome analyses supported by Co-immunoprecipitation (Co-IP) assay revealed that STY1099 protein plays a role in redox homeostasis during the peroxide stress assault via involvement in the processes of respiratory nitrate reductase, oxidoreductase activities, cellular uptake and stress response. In addition, we found that the STY1099 protein has the monopolar subcellular location and that it interacts with key cell division proteins, MinD, and FtsH, as well as with a rod shape-determining protein MerB.