Enzymatic characteristics of an ApaH‐like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from <i>Myxococcus xanthus</i>

Sasaki, Masahiro; Takegawa, Kaoru; Kimura, Yoshinobu

doi:10.1016/j.febslet.2014.07.031

Cited by 17 publications

(12 citation statements)

References 30 publications

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“…Salmonella enterica also contains ApaH and a Nudix hydrolase, YgdP, which have almost equal Ap n A hydrolase activities [5]. We have previously reported that M. xanthus recombinant ApaH exhibited high hydrolase activity towards Ap n A [18]. Thus, the specific activities of ApaH towards Ap 4 A and Ap 5 A in the presence of 1 mM Co 2+ were 16.2±0.57 and 54.7±0.60 µmol min À1 mg…”

Section: Discussionmentioning

confidence: 99%

“…In addition, LysS catalyses the production of diadenosine pentaphosphate (Ap 5 A) from Ap 4 [14], which is generated by acyl-CoA synthetase, acetyl-CoA synthetase or adenylate kinase [15][16][17]. M. xanthus contains two Ap n A hydrolases: ApaH and Nudix hydrolases; ApaH degrades Ap 4 A into two ADP molecules in the presence of Co 2+ or Mn 2+ [18].…”

Section: Introductionmentioning

confidence: 99%

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High concentrations of intracellular Ap4A and/or Ap5A in developing Myxococcus xanthus cells inhibit sporulation

et al. 2017

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Diadenosine polyphosphates (Ap n A) are thought to act as signalling molecules regulating stress responses and biofilm formation in prokaryotes. However, Ap n A function in Myxococcus xanthus remains unknown. Here, we investigated the role of Ap n A in M. xanthus, using the wild-type and Ap n A hydrolase (apaH) mutant strains exposed to various stress conditions. In both wild-type and apaH mutant cells cultured on starvation medium (CF agar), the levels of intracellular diadenosine tetraphosphate (Ap 4 A) and pentaphosphate (Ap 5 A) increased several fold during the first 16 h of development and decreased gradually thereafter. The levels of Ap 4 A and Ap 5 A in the apaH mutant were about 5-and 11-fold higher than those in the wild-type strain at 16 h, respectively. Ap n A hydrolase activity of the wild-type strain increased 1.5-fold during the first 8 h of development, and it then gradually decreased. The apaH mutant formed spores 1-2 days after the wild-type strain did, and the yield of viable spores was 5.5 % of that in the wild-type strain 5 days after inoculation onto CF agar. These results suggest the possibility that high intracellular levels of Ap 4 A and/or Ap 5 A may inhibit M. xanthus sporulation at the early stage of development and that the bacteria reduce intracellular Ap 4 A and Ap 5 A accumulation through Ap n A hydrolase activity.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High concentrations of intracellular Ap4A and/or Ap5A in developing Myxococcus xanthus cells inhibit sporulation

et al. 2017

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“…The gene of this proteinase -prolyl endopeptidase (produced by Myxococcus xanthus) was cloned into a food-grade recombinant Lactobacillus casei strain, thus obtaining a new tool to cure celiac disease (Alvarez-Sieiro et al 2014). Sasaki et al (2014) characterised the activities of the Myxococcus xanthus ApaHlike phosphatases PrpA and ApaH, which share homologies with both phosphoprotein phosphatases and diadenosine tetraphosphate (Ap 4 A) hydrolases. The above authors stated that PrpA and ApaH may function mainly as a tyrosine protein phosphatase and an Ap 4 A hydrolase, respectively (Sasaki et al 2014).…”

Section: Enzymatic Activitymentioning

confidence: 99%

Current trends in myxobacteria research

et al. 2015

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Myxobacteria are fascinating Gram-negative bacteria whose life cycle includes the formation of multicellular fruiting bodies that contain about 100,000 cells differentiated as asexual spores for their long-term survival. They move by gliding on surfaces, an activity that helps them carry out their primitive kind of multicellular development. Myxobacteria have multiple traits that are clearly social in nature; they move and feed socially. These processes require specific intercellular signals, thereby exhibiting a sophisticated level of the interorganismal communication. Myxobacteria are predators. Predation is social not only with respect to searching for prey (motility) but also in the killing of prey. Swarming groups of cells secrete antibiotics and bacteriolytic compounds that kill and lyse their prey, and food is thereby released. Since the last three decades, myxobacteria are known as valuable producers of secondary metabolites exhibiting various biological activities. Myxobacterial metabolites exhibit many unique structural features as well as rare or novel modes of action, making them attractive lead structures for drug development. Both genome sequencing and metabolic profiling of myxobacterial strains suggest that the diversity of myxobacterial secondary metabolism is far greater than previously appreciated. The present review discusses the structure, cytology, physiology, and ecology of myxobacteria, as well as their secondary metabolite production and social interactions.

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“…Since these substrates of Nudix hydrolases are involved in en-Ap 4 A is composed of two adenosine moieties joined by a 5¢-5¢-linked chain of four phosphates. It has been reported that Nudix hydrolases from other organisms catalyze the asymmetric cleavage of Ap 4 A to ATP and AMP in the presence of Mg 2+ or Mn 2+ (Swarbrick et al, 2004 (Sasaki et al, 2014). However, the specific activity of Nud11 for Ap 4 A and Ap 5 A was approximately 4-10-fold lower than that of M. xanthus ApaH.…”

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confidence: 98%

“…On the other hand, bacteria have two different Ap n A hydrolases, ApaH and Nudix (nucleoside diphosphate linked moiety X) (Andreeva and Kutuzov, 2004;McLennan, 2006). The ApaH hydrolase shares sequence similarity with phosphoprotein phosphatases (Andreeva and Kutuzov, 2004), and our previous study indicates that approximately 60-70% of Ap n A hydrolytic activity in M. xanthus vegetative cells is provided by ApaH (Sasaki et al, 2014).…”

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confidence: 99%