Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product

Thaller, María Cristina; Schippa, Serena; Bonci, Alessandra; Cresti, Stefania; Rossolini, Gian María

doi:10.1111/j.1574-6968.1997.tb10192.x

Cited by 50 publications

(24 citation statements)

References 16 publications

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“…In general, the starvation for inorganic phosphate stimulates the production of these enzymes in yeast, moulds and bacteria (Sreeramulu et al. 1996; Thaller et al. 1997; Pandey et al.…”

Section: Discussionmentioning

confidence: 99%

“…The molecular mass determined for the native enzyme of L. pentosus CECT 4023 differs from the ones reported for other bacteria. Most of the characterized bacterial phosphatases such as those from L. plantarum DPC 2739, Lactobacillus curvatus and enteric bacteria have a molecular mass of 100–110 kDa (Thaller et al. 1997; Abdallah et al.…”

Section: Discussionmentioning

confidence: 99%

“…The effect of the chelating agents (EDTA and o ‐phenanthroline) varies greatly depending on the concentrations. These compounds were inhibitors of phosphatases from enteric bacteria, but stimulated or had no effect on the phosphatase activities of LAB (Thaller et al. 1997; Akuzawa and Fox 1998; Abdallah et al.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of an acid phosphatase from Lactobacillus pentosus: regulation and biochemical properties

2005

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Aims: To screen for phosphatase and phytase activities in Lactobacillus isolated from diverse ecosystems and to determine the biochemical properties and the factors that regulate the synthesis of the enzyme responsible for these activities in the selected strain, Lactobacillus pentosus CECT 4023. Methods and Results: These activities were determined spectrophotometrically by using p-nitrophenyl phosphate and sodium phytate as substrates. They were maximal at the onset of the stationary phase of growth and repressed in the presence of high glucose concentration and inorganic phosphate. The enzyme responsible for these activities was an acid phosphatase (E.C.3.1.3.2.), with a molecular mass of 69 kDa. The activity was optimum at pH 5AE0 and 50°C. It hydrolysed mono-phosphorylated substrates and phytate, albeit at lower rates. It was inhibited by iodoacetic acid, phenyl-methylsulphonyl fluoride, di-sodium pyrophosphate and Ca +2 while activated by Co +2 and low concentrations of L L-ascorbic acid and EDTA. Conclusions: Lactobacillus pentosus CECT 4023 produces a nonspecific acid phosphatase that hydrolyses a number of mono-phosphorylated substrates and phytate. Significance and Impact of the Study: The results suggest that the phosphatase from L. pentosus CECT 4023 could partly contribute to reduce the phosphorylation degree of phytate and its derivatives and, thereby, their anti-nutrient properties during fermentation processes.

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“…In general, the starvation for inorganic phosphate stimulates the production of these enzymes in yeast, moulds and bacteria (Sreeramulu et al. 1996; Thaller et al. 1997; Pandey et al.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Characterization of an acid phosphatase from Lactobacillus pentosus: regulation and biochemical properties

2005

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“…Proteins with differential abundance in E. coli MG1655 ibpAyfp (pLHR) and ibpA-yfp (pRK767) include the metabolic enzymes AphA and TdcF and the oxidoreductases GhrB and OsmC. The class B acid phosphatase AphA dephosphorylates phosphomonoesters to transfer the phosphate to hydroxyl groups (Thaller et al, 1997); TdcF interacts with toxic 2-ketobutyrate to prevent its accumulation (Burman et al, 2007). The glyoxylate reductase GhrB oxidizes glycolate to glyoxylate as part of the biosynthesis of serine (Nuñez et al, 2001).…”

Section: Differential Abundance Of Proteins In Inclusion Bodiesmentioning

confidence: 99%

Heat and Pressure Resistance in Escherichia coli Relates to Protein Folding and Aggregation

Mercer

Behr

et al. 2020

Front. Microbiol.

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The locus of heat resistance (LHR) confers extreme heat resistance in Escherichia coli. This study explored the role of the LHR in heat and pressure resistance of E. coli, as well as its relationship with protein folding and aggregation in vivo. The role of LHR was investigated in E. coli MG1655 and the pressure resistant E. coli LMM1010 expressing an ibpA-yfp fusion protein to visualize inclusion bodies by fluorescence microscopy. The expression of proteins by the LHR was determined by proteomic analysis; inclusion bodies of untreated and treated cells were also analyzed by proteomics, and by fluorescent microscopy. In total, 11 proteins of LHR were expressed: sHSP20, ClpK GI , sHSP, YdfX1 and YdfX2, HdeD, KefB, Trx, PsiE, DegP, and a hypothetical protein. The proteomic analysis of inclusion bodies revealed a differential abundance of proteins related to oxidative stress in strains carrying the LHR. The LHR reduced the presence of inclusion bodies after heat or pressure treatment, indicating that proteins expressed by the LHR prevent protein aggregation, or disaggregate proteins. This phenotype of the LHR was also conferred by expression of a fragment containing only sHSP20, ClpK GI , and sHSP. The LHR and the fragment encoding only sHSP20, ClpK GI , and sHSP also enhanced pressure resistance in E. coli MG1655 but had no effect on pressure resistance of E. coli LMM1010. In conclusion, the LHR confers pressure resistance to some strains of E. coli, and reduces protein aggregation. Pressure and heat resistance are also dependent on additional LHR-encoded functions.

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“…Furthermore, HobH was described as a component of the outer membrane involved in hemimethylated oriC binding based on studies performed with a LacZ-HobH fusion protein [11]. Later, it was reported that HobH is a non-specific acid phosphatase and it was termed NAP [64]. NAP protein was purified to near homogeneity and its hemimethylated DNA binding activity was examined [65].…”

Section: Binding Of Hemimethylated Oric To the Outer Membranementioning

confidence: 99%

Compartmentalization of prokaryotic DNA replication

2005

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It becomes now apparent that prokaryotic DNA replication takes place at specific intracellular locations. Early studies indicated that chromosomal DNA replication, as well as plasmid and viral DNA replication, occurs in close association with the bacterial membrane. Moreover, over the last several years, it has been shown that some replication proteins and specific DNA sequences are localized to particular subcellular regions in bacteria, supporting the existence of replication compartments. Although the mechanisms underlying compartmentalization of prokaryotic DNA replication are largely unknown, the docking of replication factors to large organizing structures may be important for the assembly of active replication complexes. In this article, we review the current state of this subject in two bacterial species, Escherichia coli and Bacillus subtilis, focusing our attention in both chromosomal and extrachromosomal DNA replication. A comparison with eukaryotic systems is also presented.

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Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product

Cited by 50 publications

References 16 publications

Characterization of an acid phosphatase from Lactobacillus pentosus: regulation and biochemical properties

Characterization of an acid phosphatase from Lactobacillus pentosus: regulation and biochemical properties

Heat and Pressure Resistance in Escherichia coli Relates to Protein Folding and Aggregation

Compartmentalization of prokaryotic DNA replication

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