LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 2 of total 2

Search options

  1. Article ; Online: c-di-GMP inhibits the DNA binding activity of H-NS in Salmonella.

    Li, Shuyu / Liu, Qinmeng / Duan, Chongyi / Li, Jialin / Sun, Hengxi / Xu, Lei / Yang, Qiao / Wang, Yao / Shen, Xihui / Zhang, Lei

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 7502

    Abstract: Cyclic di-GMP (c-di-GMP) is a second messenger that transduces extracellular stimuli into cellular responses and regulates various biological processes in bacteria. H-NS is a global regulatory protein that represses expression of many genes, but how H-NS ...

    Abstract Cyclic di-GMP (c-di-GMP) is a second messenger that transduces extracellular stimuli into cellular responses and regulates various biological processes in bacteria. H-NS is a global regulatory protein that represses expression of many genes, but how H-NS activity is modulated by environmental signals remains largely unclear. Here, we show that high intracellular c-di-GMP levels, induced by environmental cues, relieve H-NS-mediated transcriptional silencing in Salmonella enterica serovar Typhimurium. We find that c-di-GMP binds to the H-NS protein to inhibit its binding to DNA, thus derepressing genes silenced by H-NS. However, c-di-GMP is unable to displace H-NS from DNA. In addition, a K107A mutation in H-NS abolishes response to c-di-GMP but leaves its DNA binding activity unaffected in vivo. Our results thus suggest a mechanism by which H-NS acts as an environment-sensing regulator in Gram-negative bacteria.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cyclic GMP/metabolism ; Second Messenger Systems ; Salmonella typhimurium/metabolism ; Gene Expression Regulation, Bacterial
    Chemical Substances bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Bacterial Proteins ; Cyclic GMP (H2D2X058MU)
    Language English
    Publishing date 2023-11-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-43442-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Autoinducer-2 and bile salts induce c-di-GMP synthesis to repress the T3SS via a T3SS chaperone.

    Li, Shuyu / Sun, Hengxi / Li, Jianghan / Zhao, Yujiao / Wang, Ruiying / Xu, Lei / Duan, Chongyi / Li, Jialin / Wang, Zhuo / Liu, Qinmeng / Wang, Yao / Ouyang, Songying / Shen, Xihui / Zhang, Lei

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 6684

    Abstract: Cyclic di-GMP (c-di-GMP) transduces extracellular stimuli into intracellular responses, coordinating a plethora of important biological processes. Low levels of c-di-GMP are often associated with highly virulent behavior that depends on the type III ... ...

    Abstract Cyclic di-GMP (c-di-GMP) transduces extracellular stimuli into intracellular responses, coordinating a plethora of important biological processes. Low levels of c-di-GMP are often associated with highly virulent behavior that depends on the type III secretion system (T3SS) effectors encoded, whereas elevated levels of c-di-GMP lead to the repression of T3SSs. However, extracellular signals that modulate c-di-GMP metabolism to control T3SSs and c-di-GMP effectors that relay environmental stimuli to changes in T3SS activity remain largely obscure. Here, we show that the quorum sensing signal autoinducer-2 (AI-2) induces c-di-GMP synthesis via a GAPES1 domain-containing diguanylate cyclase (DGC) YeaJ to repress T3SS-1 gene expression in Salmonella enterica serovar Typhimurium. YeaJ homologs capable of sensing AI-2 are present in many other species belonging to Enterobacterales. We also reveal that taurocholate and taurodeoxycholate bind to the sensory domain of the DGC YedQ to induce intracellular accumulation of c-di-GMP, thus repressing the expression of T3SS-1 genes. Further, we find that c-di-GMP negatively controls the function of T3SSs through binding to the widely conserved CesD/SycD/LcrH family of T3SS chaperones. Our results support a model in which bacteria sense changes in population density and host-derived cues to regulate c-di-GMP synthesis, thereby modulating the activity of T3SSs via a c-di-GMP-responsive T3SS chaperone.
    MeSH term(s) Bile Acids and Salts ; Cyclic GMP/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Salmonella typhimurium/genetics ; Salmonella typhimurium/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Gene Expression Regulation, Bacterial ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms
    Chemical Substances bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Bile Acids and Salts ; Cyclic GMP (H2D2X058MU) ; Escherichia coli Proteins ; Molecular Chaperones ; Bacterial Proteins
    Language English
    Publishing date 2022-11-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-34607-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top