Two genes encoding uracil phosphoribosyltransferase are present in Bacillus subtilis

Martinussen, Jan; Glaser, Philippe; Andersen, Paal Skytt; Saxild, Hans Henrik

doi:10.1128/jb.177.1.271-274.1995

Cited by 44 publications

(42 citation statements)

References 13 publications

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“…This may be a transcription terminator for the preceding upp gene (36). A similar structure is found just after the atpC gene and may be the transcription terminator of the atp operon.…”

Section: Resultsmentioning

confidence: 93%

Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants

et al. 1994

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We cloned and sequenced an operon of nine genes coding for the subunits of the Bacillus subtilis FOF, ATP synthase. The arrangement of these genes in the operon is identical to that of the atp operon from Escherichia coli and from three other Bacillus species. The deduced amino acid sequences of the nine subunits are very similar to their counterparts from other organisms. We constructed two B. subtilis strains from which different parts of the atp operon were deleted. These B. subtilis atp mutants were unable to grow with succinate as the sole carbon and energy source. ATP was synthesized in these strains only by substrate-level phosphorylation. The two mutants had a decreased growth yield (43 and 56% of the wild-type level) and a decreased growth rate (61 and 66% of the wild-type level), correlating with a twofold decrease of the intracellular ATP/ADP ratio. In the absence of oxidative phosphorylation, B. subtilis increased ATP synthesis through substrate-level phosphorylation, as shown by the twofold increase of by-product formation (mainly acetate). The increased turnover of glycolysis in the mutant strain presumably led to increased synthesis of NADH, which would account for the observed stimulation of the respiration rate associated with an increase in the expression of genes coding for respiratory enzymes. It therefore appears that B. subtilis and E. coli respond in similar ways to the absence of oxidative phosphorylation.ATP plays a central role in energy transduction in living organisms. Although some ATP is synthesized in aerobiosis by soluble enzyme systems like glycolytic enzymes that perform substrate-level phosphorylation, most is synthesized by membrane-bound enzyme complexes through oxidative phosphorylation. The energy-transducing membranes, where these complexes are found, are the plasma membrane of prokaryotic cells, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. ATP synthesis from ADP and Pi is catalyzed by the ATP synthase complex and is driven by the proton gradient. This gradient is generated by respiration in mitochondria and respiring bacteria and by photosynthesis in chloroplasts and photosynthetic bacteria.ATP

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“…This may be a transcription terminator for the preceding upp gene (36). A similar structure is found just after the atpC gene and may be the transcription terminator of the atp operon.…”

Section: Resultsmentioning

confidence: 93%

Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants

et al. 1994

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“…Uracil phosphoribosyltransferase (Upp) functions to regulate entry into the pyrimidine salvage pathway commonly induced by starvation conditions, whereas SerA (D-3-phosphoglycerate dehydrogenase) regulates the cellular levels of 3-phosphoglycerate from serine. Neither has an apparent role in STM pathogenesis (47,48).…”

Section: Figure 3 Validation Of Ms Results By Western Blot Analysismentioning

confidence: 99%

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Shi

Adkins

Coleman

et al. 2006

Journal of Biological Chemistry

135

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To evade host resistance mechanisms, Salmonella enterica serovar Typhimurium (STM), a facultative intracellular pathogen, must alter its proteome following macrophage infection. To identify new colonization and virulence factors that mediate STM pathogenesis, we have isolated STM cells from RAW 264.7 macrophages at various time points following infection and used a liquid chromatography-mass spectrometry-based proteomic approach to detect the changes in STM protein abundance. Because host resistance to STM infection is strongly modulated by the expression of a functional host-resistant regulator, i.e. natural resistanceassociated macrophage protein 1 (Nramp1, also called Slc11a1), we have also examined the effects of Nramp1 activity on the changes of STM protein abundances. A total of 315 STM proteins have been identified from isolated STM cells, which are largely housekeeping proteins whose abundances remain relatively constant during the time course of infection. However, 39 STM proteins are strongly induced after infection, suggesting their involvement in modulating colonization and infection. Of the 39 induced proteins, 6 proteins are specifically modulated by Nramp1 activity, including STM3117, as well as STM3118 -3119 whose time-dependent abundance changes were confirmed using Western blot analysis. Deletion of the gene encoding STM3117 resulted in a dramatic reduction in the ability of STM to colonize wild-type RAW 264.7 macrophages, demonstrating a critical involvement of STM3117 in promoting the replication of STM inside macrophages. The predicted function common for STM3117-3119 is biosynthesis and modification of the peptidoglycan layer of the STM cell wall.

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“…Thus, PyrR would be relatively ineffective in uracil salvage. However, B. subtilis (36) and B. caldolyticus (7) pyrR genes have been shown to encode functional UPRTases in vivo.…”

Section: Implications For the Mechanism Of Other Prtases-thementioning

confidence: 99%

Kinetic Studies of the Uracil Phosphoribosyltransferase Reaction Catalyzed by the Bacillus subtilis Pyrimidine Attenuation Regulatory Protein PyrR

Grabner

Switzer

2003

Journal of Biological Chemistry

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for PyrR that include a kinetically irreversible conformational change after binding of PRPP but before uracil binding were shown to account for the Ping Pong pattern of the enzyme. This mechanism was supported by the following experimental observations. The reverse reaction was extremely slow with a catalytic rate constant 3300 times smaller than for the forward reaction. Patterns of product inhibition of the forward reaction were consistent with a version of the irreversible conformational change model in which PyrR returns to the unliganded conformation before dissociation of UMP and were inconsistent with several other kinetic mechanisms. UMP and phosphoribosylpyrophosphate were shown by equilibrium dialysis to bind to free PyrR (dissociation constants of 27 ؎ 3 and 18 ؎ 2 M, respectively), but uracil and PP i did not bind at equilibrium concentrations up to 750 M. We propose that the conformational change kinetic model developed for PyrR can also account for numerous other reports of Ping Pong kinetics for various phosphoribosyltransferases that do not form the phosphoribosyl-enzyme intermediate predicted by classic Ping Pong kinetics.

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Two genes encoding uracil phosphoribosyltransferase are present in Bacillus subtilis

Cited by 44 publications

References 13 publications

Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants

Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and characterization of atp mutants

Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages

Kinetic Studies of the Uracil Phosphoribosyltransferase Reaction Catalyzed by the Bacillus subtilis Pyrimidine Attenuation Regulatory Protein PyrR

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