Metal oxide hetero-nanostructures have widely been used as the core part of chemical gas sensors. To improve the dispersion state of each constituent and the poor stability that exists in heterogeneous gas sensing materials, a uniaxial electro-spinning method combined with calcination was applied to synthesize pure SnO₂ and three groups of WO₃/SnO₂ (WO₃ of 0.1, 0.3, 0.9 wt%) hetero-nanofibers (HNFs) in our work. A series of characterizations prove that the products present hollow and fibrous structures composed of even nanoparticles while WO₃ is uniformly distributed into the SnO₂ matrix. Gas sensing tests display that the WO₃/SnO₂ (0.3 wt%) sensor not only exhibits the highest response (30.28) and excellent selectivity to acetone vapor at the lower detection temperature (170°C), 6 times higher than that of pure SnO₂ (5.2), but still achieves a considerable response (4.7) when the acetone concentration is down to 100 ppb with the corresponding response/recovery times of 50/200 s, respectively. Such structure obviously enhances the gas sensing performance toward acetone which guides the construction of a highly sensitive acetone sensor. Meanwhile, the enhancement mechanism of such a special sensor is also discussed in detail.

Cold Shock Proteins (Csps) are multifunctional regulators critical for bacterial stress adaptation. While Csps are known to regulate biofilm formation and low-temperature growth in some species, their roles in mycobacteria remain unclear. Here, we explored the functions of three Csps (CspA1, CspA2, and CspB) in Mycobacterium smegmatis. We found that CspA1 promotes biofilm formation and isoniazid (INH) resistance but negatively affects oxidative stress resistance. In contrast, CspB promotes biofilm formation, whereas CspA2 appears functionally redundant in this process. Notably, CspB and CspA2 do not contribute redundantly to oxidative stress resistance. Proteomic analysis revealed that CspA1 significantly modulates the expression of key metabolic and stress-response proteins, including WhiB3 and KatG. Our findings establish CspA1 as a key regulatory factor in mycobacteria, linking metabolic adaptation to biofilm-associated drug resistance and oxidative defense.

The Structural Maintenance of Chromosomes complex 5/6 (SMC-5/6) safeguards genome stability by coordinating DNA replication, repair, and chromosome organization. Although prior studies have advanced understanding of SMC-6, a domain-resolved view of its functions in vivo, particularly in multicellular organisms, remains incomplete. Because the non-SMC subunit NSE-1 localizes at the SMC-5/6 head interface and reflects complex integrity, we used NSE-1::GFP nuclear localization as a visual readout in an ethyl methanesulfonate (EMS)-based forward genetic screen in Caenorhabditis elegans (C. elegans). We identified three new smc-6 alleles—smc-6(wsh34), smc-6(wsh35), and smc-6(wsh36) through single-nucleotide polymorphism (SNP) mapping and whole-genome sequencing. smc-6(wsh34) and smc-6(wsh35) affect the N-terminal ATPase domain, whereas smc-6(wsh36) lies in the hinge region. ATPase-domain mutants exhibited reduced fertility, decreased progeny viability, hypersensitivity to methyl methanesulfonate and cisplatin, and strong induction of the pro-apoptotic genes egl-1 and ced-13. In contrast, the hinge mutant exhibited moderate fertility defects and partial sensitivity to DNA damage reagents. Structural modeling suggests that the R103 truncation disrupts the SMC-5/6 head interface, whereas the P514L substitution alters hinge dynamics. Together, these findings reveal a functional hierarchy in SMC-6, with the ATPase domain governing repair-associated energy-dependent processes and the hinge maintaining structural integrity.