UbK is Involved in the Resistance of Bacillus Subtilis to Oxidative Stress

El-Khoury, Takla G.; Nguyen, Hai Duc; Candusso, Marie-Pierre; Attieh, Jihad; Jault, Jean‐Michel

doi:10.1007/s00284-020-02239-1

Cited by 3 publications

(4 citation statements)

References 52 publications

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“…UbK proteins have a number of conserved domains including a canonical Walker A motif, also found in BY‐kinases, along with HxDxYR, SPT/S, and EW motifs. This family was originally classified as ATPases, and currently only two have been confirmed as kinases (El‐Khoury et al., 2020; Nguyen et al., 2017; Pelletier et al., 2019). We report here the identification of a functional UbK enzyme in the oral anaerobic periodontal pathogen, P. gingivalis .…”

Section: Discussionmentioning

confidence: 99%

“…In addition to the conserved physiological role of UbKs involving the t 6 A modification of a subset of tRNAs (Deutsch et al., 2012; Lauhon, 2012), UbKs have been reported to control stress resistance and maintenance of growth and cell morphology (El‐Khoury et al., 2020; Nguyen et al., 2017; Pelletier et al., 2019). In another oral organism, Streptococcus mutans , the UbK homolog, BrpB/TsaE, controls cell division, stress responses, and biofilm formation (Bitoun et al., 2014).…”

Section: Discussionmentioning

confidence: 99%

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Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator

Perpich

Yakoumatos

Johns

et al. 2021

Molecular Oral Microbiology

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Phosphorylation of proteins is a key component of bacterial signaling systems that can control important functions such as community development and virulence. We report here the identification of a Ubiquitous bacterial Kinase (UbK) family member, designated UbK1, in the anaerobic periodontal pathogen, Porphyromonas gingivalis. UbK1 contains conserved SPT/S, Hanks‐type HxDxYR, EW, and Walker A motifs, and a mutation analysis established the Walker A domain and the Hanks‐type domain as required for both autophosphorylation and transphosphorylation. UbK1 autophosphorylates on the proximal serine in the SPT/S domain as well as the tyrosine residue within the HxDxYR domain and the tyrosine residue immediately proximal, indicating both serine/threonine and tyrosine specificity. The orphan two‐component system response regulator (RR) RprY was phosphorylated on Y41 in the receiver domain by UbK1. The ubk1 gene is essential in P. gingivalis; however, overexpression of UbK1 showed that UbK1‐mediated phosphorylation of RprY functions predominantly to augment its properties as a transcriptional enhancer. These results establish that P. gingivalis possesses an active UbK kinase in addition to a previously described Bacterial Tyrosine family kinase. The RR RprY is identified as the first transcriptional regulator controlled by a UbK enzyme.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator

Perpich

Yakoumatos

Johns

et al. 2021

Molecular Oral Microbiology

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“…(iii) Oxidative stress. UbK enzymes can control stress responses in other organisms [ 28 , 29 ]. In P. gingivalis , Ubk1 phosphorylates and modulates the activity of the orphan response regulator (RR) RprY [ 17 ].…”

Section: Tyrosine Kinase and Phosphatase Functions In P Gin...mentioning

confidence: 99%

Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle

Lamont

Miller

2022

Front. Oral. Health

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Tyrosine phosphorylation modifies the functionality of bacterial proteins and forms the basis of a versatile and tunable signal transduction system. The integrated action of tyrosine kinases and phosphatases controls bacterial processes important for metabolism and virulence. Porphyromonas gingivalis, a keystone pathogen in periodontal disease, possesses an extensive phosphotyrosine signaling network. The phosphorylation reaction is catalyzed by a bacterial tyrosine (BY) kinase, Ptk1, and a Ubiquitous bacterial Kinase UbK1. Dephosphorylation is mediated by a low-molecular-weight phosphatase, Ltp1 and a polymerase and histidinol phosphatase, Php1. Phosphotyrosine signaling controls exopolysaccharide production, gingipain activity, oxidative stress responses and synergistic community development with Streptococcus gordonii. Additionally, Ltp1 is secreted extracellularly and can be delivered inside gingival epithelial cells where it can override host cell signaling and readjust cellular physiology. The landscape of coordinated tyrosine kinase and phosphatase activity thus underlies the adaptive responses of P. gingivalis to both the polymicrobial environment of bacterial communities and the intracellular environment of gingival epithelial cells.

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“…Concerning the cellular role of Ubk in B. subtilis, it was firstly described as an essential protein [75]. Reinvestigation of its cellular role showed that ubk gene is not essential [76] but its deletion or mutations induce a delay of growth and a modification of resistance to oxidative stress [77]. However, here again, the mechanism by which Ubk regulates resistance to oxidative stress as well as the consequence of YdiE phosphorylation are unknown.…”

Section: Ubk Constitutes a New Family Of Conserved Apkmentioning

confidence: 99%

Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis

Zhang

Pompeo

Galinier

2021

Research in Microbiology

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UbK is Involved in the Resistance of Bacillus Subtilis to Oxidative Stress

Cited by 3 publications

References 52 publications

Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator

Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator

Tyrosine Kinases and Phosphatases: Enablers of the Porphyromonas gingivalis Lifestyle

Overview of protein phosphorylation in bacteria with a main focus on unusual protein kinases in Bacillus subtilis

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