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SJTU Researchers Published Research Article in Cell Discovery

March 29, 2021      Author:

Recently, Dr. Zhou Zikang and Prof. Tang Hongzhi from the State Key Laboratory of Microbial Metabolism, SJTU School of Life Sciences and Biotechnology published a collaborative research article on the website of Cell Discovery (2021, 7:1-12). Titled “A cold shock protein promotes high-temperature microbial growth through binding to diverse RNA species”, the article revealed the molecular mechanism of the cold shock protein CspL facilitating cells growth in high-temperature environment.


The team found the global protective role of the cold chock protein CspL on RNA under cellular high-temperature stress. Microbial cells must maintain stable physiological and biochemical functions under various stress conditions. Elevated temperature disrupts the original intracellular homeostasis, interfering with normal physiological functions and altering cell structure. Improving microbial tolerance to high temperatures has potential applications, such as reducing the risk of contamination in open fermentations, and thus reducing production costs. A novel cold shock protein CspL derived from Bacillus coagulans 2-6 was identified in the excavation of high-temperature tolerant components, and it was confirmed that CspL binds mRNA and protects its conformation, which in turn promotes cell growth.


This research was supported by the National Key R&D Program of China (No. 2018YFA0901200) and the Shanghai Outstanding Academic Leaders Program (No. 20XD1421900). Dr. Zhou Zikang and Prof. Tang Hongzhi are the co-first authors, and Prof. Tang Hongzhi is also the co-corresponding author of the paper. Several members of Prof. Bai Linquan’s team from SJTU School of Life Sciences and Biotechnology and Prof. Sun Yuhui’s team from Wuhan University also participated in the research.

Source: School of Life Sciences and Bio Technology, SJTU

Translated by Chen Chen

Proofread by Xiao Yangning, Fu Yuhe


Endowing mesophilic microorganisms with high-temperature resistance is highly desirable for industrial microbial fermentation. Here, we report a cold-shock protein (CspL) that is an RNA chaperone protein from a lactate producing thermophile strain (Bacillus coagulans 2–6), which is able to recombinantly confer strong high-temperature resistance to other microorganisms. Transgenic cspL expression massively enhanced high-temperature growth of Escherichia coli (a 2.4-fold biomass increase at 45 °C) and eukaryote Saccharomyces cerevisiae (a 2.6-fold biomass increase at 36 °C). Importantly, we also found that CspL promotes growth rates at normal temperatures. Mechanistically, bio-layer interferometry characterized CspL’s nucleotide-binding functions in vitro, while in vivo we used RNA-Seq and RIP-Seq to reveal CspL’s global effects on mRNA accumulation and CspL’s direct RNA binding targets, respectively. Thus, beyond establishing how a cold-shock protein chaperone provides high-temperature resistance, our study introduces a strategy that may facilitate industrial thermal fermentation.