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The calcium-sensing receptor (CAS), as a chloroplast thylakoid membrane protein, is involved in the process of external Ca2+-induced cytosolic Ca2+ increase in plants. However, the underlying mechanism regulating this process is lacking. Furthermore, recent evidence suggests that CAS may perform additional roles in plants. Here, we provided an update covering the multiple roles of CAS in stomatal movement regulation and Ca2+ signaling in plants. We also analyzed the possible phosphorylation mechanism of CAS by light and discuss the role of CAS in abiotic stress (drought, salt stress) and biotic stresses (plant immune signaling). Finally, we proposed a perspective for future experiments that are required to fill gaps in our understanding of the biological function of CAS in plants. • Calcium-sensing receptor (CAS) is a photoregulated phosphorylated protein located on chloroplast thylakoid membrane. • CAS involved in the process of external Ca2+-induced cytosolic Ca2+ increase in plants. • CAS involved in light signal transduction, stomatal movement regulation and drought tolerance. • CAS-modulated MAPK signaling involved plastid-nucleus communication. • CAS-modulated SA signaling mediated plant immune signaling. [ABSTRACT FROM AUTHOR]

Mycotoxins are representative contaminants causing food losses and food safety problems worldwide. Thymol can effectively inhibit pathogen infestation and aflatoxin accumulation during grain storage, but high volatility limits its application. Here, a thymol-betaine co-crystal system was synthesized through grinding-induced self-assembly. The THY-TMG co-crystal exhibited excellent thermal stability with melting point of 91.2 °C owing to abundant intermolecular interactions. Remarkably, after 15 days at 30 °C, the release rate of thymol from co-crystal was only 55%, far surpassing that of pure thymol. Notably, the co-crystal demonstrated the ability to bind H 2 O in the environment while controlling the release of thymol, essentially acting as a desiccant. Moreover, the co-crystals effectively inhibited the growth of Aspergillus flavus and the biosynthesis of aflatoxin B 1. In practical terms, the THY-TMG co-crystal was successful in preventing AFB 1 contamination and nutrients loss in peanuts, thereby prolonging their shelf-life under conditions of 28 °C and 70% RH. • Crystal engineering is an emerging technology for extending the shelf life of food. • A novel THY-TMG co-crystal was synthesized by grinding induced self-assembly. • THY-TMG have excellent controlled release and hygroscopic properties. • THY-TMG significantly inhibited the growth and AFB 1 biosynthesis of A. flavus. • THY-TMG prevented AFB 1 contamination and nutrient loss in long term storage of peanuts. [ABSTRACT FROM AUTHOR]

Abstract: The genome of Arabidopsis thaliana contains seven Hsp90 family genes. Three organellar and two cytosolic AtHsp90 isoforms were characterized by functionally expressing them in a temperature-sensitive Hsp90 mutant and a conditional Hsp90-null mutant of Saccharomyces cerevisiae. The cytosolic AtHsp90-1 and AtHsp90-2 showed function similar to that of yeast in chaperoning roles; they could support the growth of yeast mutants at both permissive and non-permissive temperature. Neither the full-length nor mature forms of chloroplast-located AtHsp90-5, mitochondria-located AtHsp90-6 and endoplasmic reticulum (ER)-located AtHsp90-7 could complement the yeast Hsp90 proteins. The cytosolic AtHsp90s could stabilize the biomembrane of the temperature-sensitive Hsp90 mutant strains under stress conditions, while the organellar AtHsp90s could not protect the biomembrane of the temperature-sensitive Hsp90 mutant strains. Yeast two-hybrid results showed that either pre-protein or mature forms of organellar AtHsp90s could interact with cofactors cpHsp70, Hsp70, Hsp70t-2, Cyp40, p23 and a substrate protein of NOS, while cytosolic AtHsp90s could not interact with them. These results suggest that organellar and cytosolic AtHsp90s possibly work through different molecular mechanisms in forming chaperone complexes and performing their functional roles. [Copyright &y& Elsevier]