Tyrosine kinase activity in <i>Pseudomonas</i> aeruginosa

South, Suzanne L.; Nichols, R. Jeremy; Montie, Thomas C.

doi:10.1111/j.1365-2958.1994.tb01078.x

Cited by 21 publications

(14 citation statements)

References 27 publications

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“…The Ptk of P. syringae could not phosphorylate the synthetic substrate poly(Glu:Tyr), but could do so on peptide substrates, PKS 1 and PKS 2, corresponding to the tyrosine phosphorylation sites of eukaryotic proteins p34 dP and gastrin, respectively. The Ptk of P. aeruginosa, on the other hand, could utilise poly(Glu: Tyr) as a substrate for tyrosine phosphorylation in vitro [29,30]. In a recent study, however, a puri¢ed membrane-associated Ptk of A. johnsonii has been shown to be incapable of phosphorylating synthetic poly(Glu:Tyr) or angiotensin II as substrates [31].…”

Section: Discussionmentioning

confidence: 99%

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Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae

Jagtap

1999

FEMS Microbiology Letters

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The Antarctic psychrotrophic bacterium Pseudomonas syringae contains a 66-kDa cytoplasmic protein which was found to be phosphorylated on a tyrosine residue [Ray, M.K. et al. (1994) FEMS Microbiol. Lett. 122, pp. 49^54]. To investigate the nature of the cytoplasmic protein tyrosine kinase and its role in the bacterial physiology, we carried out some biochemical studies of the enzyme in vitro in the presence of exogenous peptide substrates and expression studies in vivo at low and high temperature during various phases of growth. The results suggest that the protein tyrosine kinase associated with the cytoplasmic fraction of the bacterium has certain similarities and dissimilarities with the known eukaryotic tyrosine kinases. The protein tyrosine kinase could phosphorylate exogenous substrate corresponding to the N-terminal peptide of p34 dP kinase but could not do so on poly(Glu:Tyr). The enzyme could not be inhibited by genistein, staurosporine and dimethyl aminopurine, but could be inhibited by piceatannol which is a known competitive inhibitor of the peptide binding site of mammalian protein tyrosine kinases. The enzyme activity in the cytoplasm is uniquely inhibited by sodium orthovanadate (IC SH =20 WM) which is a known protein tyrosine phosphatase inhibitor. The expression studies show that the enzyme is produced more at a higher temperature (22³C) of growth than at lower temperature (4³C) and during the stationary phase of growth of P. syringae. z

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Section: Discussionmentioning

confidence: 99%

“…For example, the £agellar ¢lament protein of P. aeruginosa can be phosphorylated by Ptk which is located in the cell envelope [29,30]. The Ptk activities of A. johnsonii and P. solanacearum are also associated with the cell membrane [5,32].…”

Section: Discussionmentioning

confidence: 99%

Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae

Jagtap

1999

FEMS Microbiology Letters

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“…Therapeutic targets: a novel paradigm 3. Concluding comments being made that tyrosine phosphorylation was absent from bacteria [9], it is now clear that this is not the case [10][11][12][13][14][15][16][17][18]. For example, the autophosphorylation of PutA in Salmonella typhimurium on STY residues modulates its repression of the proline utilisation operon and its degradation of proline to glutamate [19].…”

Section: Therapeutic Targets: a Novel Paradigmmentioning

confidence: 98%

Tyrosine phosphorylation in Escherichia coli has implications for the manipulation of intracellular signalling and structure in antibacterial therapies: the Jekyll and Hyde approach

Norris

Freestone

Grant

et al. 1999

Emerging Therapeutic Targets

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“…[23], exopolysaccharide secretion in Escherichia coli [9], capsule production in Streptococcus pneumoniae [24] and Klebsiella pneumonia [25] and flagellin export in Pseudomonas spp. [26]. Whitmore and Lamont [27] have reviewed the role of PTPs in bacterial virulence.…”

Section: Introductionmentioning

confidence: 99%

Nitropropenyl Benzodioxole, An Anti-Infective Agent with Action as a Protein Tyrosine Phosphatase Inhibitor

White¹,

Nicoletti²,

Borland³

2014

TOMCJ

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We report on the activities of a broad spectrum antimicrobial compound,nitropropenyl benzodioxole (NPBD) which are of relevance to its potential as an anti-infective drug. These investigations support the proposal that a major mechanism of NPBD is action as a tyrosine mimetic, competitively inhibiting bacterial and fungal protein tyrosine phosphatases (PTP).NPBD did not affect major anti-bacterial drug targets, namely, ATP production, cell wall or cell membrane integrity, or transcription and translation of RNA. NPBD inhibited bacterial YopH and human PTP1B and not human CD45 in enzyme assays. NPBD inhibited PTP-associated bacterial virulence factors, namely, endospore formation in Bacillus cereus, prodigiosin secretion in Serratia marcescens, motility in Proteus spp., and adherence and invasion of mammalian cells by Yersinia enterocolitica. NPBD acts intracellularly to inhibit the early development stages of the Chlamydia trachomatis infection cycle in mammalian cells known to involve sequestration of host cell PTPs. NPBD thus both kills pathogens and inhibits virulence factors relevant to early infection, making it a suitable candidate for development as an anti-infective agent, particularly for pathogens that enter through, or cause infections at, mucosal surfaces. Though much is yet to be understood about bacterial PTPs, they are proposed as suitable anti-infective targets and have been linked to agents similar to NPBD. The structural and functional diversity and heterogeneous distribution of PTPs across microbial species make them suitably selective targets for the development of both broadly active and pathogen-specific drugs.

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Tyrosine kinase activity in Pseudomonas aeruginosa

Cited by 21 publications

References 27 publications

Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae

Studies on the cytoplasmic protein tyrosine kinase activity of the Antarctic psychrotrophic bacterium Pseudomonas syringae

Tyrosine phosphorylation in Escherichia coli has implications for the manipulation of intracellular signalling and structure in antibacterial therapies: the Jekyll and Hyde approach

Nitropropenyl Benzodioxole, An Anti-Infective Agent with Action as a Protein Tyrosine Phosphatase Inhibitor

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