Interacting proteins of the essential two‐component system YycFG in <i>Bacillus subtilis</i>

Wu, Xuanang; Song, Qi; Han, Aidong

doi:10.1002/jobm.201800701

Cited by 3 publications

(2 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…YycFG is reported to modulate Staphylococcus epidermidis biofilm formation in an ica -dependent manner ( Xu et al, 2017 ). In Bacillus subtilis , YycFG is directly involved in regulation of cell wall synthesis and modification ( Wu et al, 2019 ). The YycG protein acts as a sensor to respond to environmental signals, and YycF can directly regulate different sets of vital functional genes by binding to promoter regions ( Winkler and Hoch, 2008 ).…”

Section: Discussionmentioning

confidence: 99%

CodY is modulated by YycF and affects biofilm formation in Staphylococcus aureus

Qin

Deng

et al. 2022

Front. Microbiol.

View full text Add to dashboard Cite

BackgroundStaphylococcus aureus (S. aureus) is the leading cause of various infective diseases, including topical soft tissue infections. The goals of this study were to investigate the roles of YycF and CodY in the regulation of biofilm formation and pathogenicity.MethodsElectrophoretic mobility shift assay (EMSA) was conducted to validate the bound promoter regions of YycF protein. We constructed the codY up-regulated or down-regulated S. aureus mutants. The biofilm biomass was determined by crystal violet microtiter assay and scanning electron microscopy (SEM). Quantitative RT-PCR analysis was used to detect the transcripts of biofilm-related genes. The live and dead cells of S. aureus biofilm were also investigated by confocal laser scanning microscopy (CLSM). We constructed an abscess infection in Sprague Dawley (SD) rat models to determine the effect of CodY on bacterial pathogenicity. We further used the RAW264.7, which were cocultured with S. aureus, to evaluate the effect of CodY on macrophages apoptosis.ResultQuantitative RT-PCR analyses reveled that YycF negatively regulates codY expression. EMSA assays indicated that YycF protein directly binds to the promoter regions of codY gene. Quantitative RT-PCR confirmed the construction of dual- mutant stains codY + ASyycF and codY-ASyycF. The SEM results showed that the biofilm formation in the codY + ASyycF group was sparser than those in the other groups. The crystal violet assays indicated that the codY + ASyycF group formed less biofilms, which was consistent with the immunofluorescence results of the lowest live cell ration in the codY + ASyycF group. The expression levels of biofilm-associated icaA gene were significantly reduced in the codY + strain, indicating codY negatively regulates the biofilm formation. Furthermore, CodY impedes the pathogenicity in a rat-infection model. After cocultured with bacteria or 4-h in vitro, the apoptosis rates of macrophage cells were lowest in the codY + group.ConclusionsYycF negatively regulate the expression of codY. By interaction with codY, YycF could modulate S. aureus biofilm formation via both eDNA- dependent and PIA- dependent pathways, which can be a significant target for antibiofilm. CodY not only impedes the pathogenicity but also has a role on immunoregulation. Thus, the current evidence may provide a supplementary strategy for managing biofilm infections.

show abstract

Section: Discussionmentioning

confidence: 99%

CodY is modulated by YycF and affects biofilm formation in Staphylococcus aureus

Qin

Deng

et al. 2022

Front. Microbiol.

View full text Add to dashboard Cite

show abstract

“…In addition to unique sensor characteristics, WalK is a focus that orchestrates the expression of a network of components that are important for bacterial metabolism and virulence ( Poupel et al, 2018 ; Wu et al, 2019 ), as well as essential components of cell division ( Fukushima et al, 2011 ; Stamsas et al, 2017 ; Zucchini et al, 2018 ). Such a focal activity renders WalRK as a target for antimicrobial development.…”

Section: Discussionmentioning

confidence: 99%

The W-Acidic Motif of Histidine Kinase WalK Is Required for Signaling and Transcriptional Regulation in Streptococcus mutans

Kong

Sang

et al. 2022

Front. Microbiol.

Self Cite

View full text Add to dashboard Cite

In Streptococcus mutans, we find that the histidine kinase WalK possesses the longest C-terminal tail (CTT) among all 14 TCSs, and this tail plays a key role in the interaction of WalK with its response regulator WalR. We demonstrate that the intrinsically disordered CTT is characterized by a conserved tryptophan residue surrounded by acidic amino acids. Mutation in the tryptophan not only disrupts the stable interaction, but also impairs the efficient phosphotransferase and phosphatase activities of WalRK. In addition, the tryptophan is important for WalK to compete with DNA containing a WalR binding motif for the WalR interaction. We further show that the tryptophan is important for in vivo transcriptional regulation and bacterial biofilm formation by S. mutans. Moreover, Staphylococcus aureus WalK also has a characteristic CTT, albeit relatively shorter, with a conserved W-acidic motif, that is required for the WalRK interaction in vitro. Together, these data reveal that the W-acidic motif of WalK is indispensable for its interaction with WalR, thereby playing a key role in the WalRK-dependent signal transduction, transcriptional regulation and biofilm formation.

show abstract

Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages

Gangwal

Kumar

Sangwan

et al. 2023

FEMS Microbiology Reviews

View full text Add to dashboard Cite

Protein phosphorylation is a universal mechanism regulating a wide range of cellular responses across all domains of life. The antagonistic activities of kinases and phosphatases can orchestrate the life cycle of an organism. The availability of bacterial genome sequences, particularly Bacillus species, followed by proteomics and functional studies have aided in the identification of putative protein kinases and protein phosphatases, and their downstream substrates. Several studies have established the role of phosphorylation in different physiological states of Bacillus species as they pass through various life stages such as sporulation, germination, and biofilm formation. The most common phosphorylation sites in Bacillus proteins are histidine, aspartate, tyrosine, serine, threonine, and arginine residues. Protein phosphorylation can alter protein activity, structural conformational and protein-protein interactions, ultimately affecting the downstream pathways. In this review, we summarize the knowledge available in the field of Bacillus signaling, with a focus on the role of protein phosphorylation in its physiological processes.

show abstract

Interacting proteins of the essential two‐component system YycFG in Bacillus subtilis

Cited by 3 publications

References 51 publications

CodY is modulated by YycF and affects biofilm formation in Staphylococcus aureus

CodY is modulated by YycF and affects biofilm formation in Staphylococcus aureus

The W-Acidic Motif of Histidine Kinase WalK Is Required for Signaling and Transcriptional Regulation in Streptococcus mutans

Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages

Contact Info

Product

Resources

About