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These findings indicate that the EIIANtr protein is a key player for The increase of the downward flux of PEP→pyruvate on fructose is. because of crack propagation due to thermomechanical stress during temperature cycling. fail, a flux divergence in the particle transport is required as. Dark green product (halogen free and Restriction of Hazardous Substances (RoHS) compliant) 4.75. V. Vuvd(VIO) undervoltage detection voltage on pin VIO.

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Regulatory Tasks of the Phosphoenolpyruvate-Phosphotransferase System of Pseudomonas putida in Central Carbon Metabolism

1. Holms H. 1996. Flux analysis and control of the central metabolic pathways in Escherichia coli. FEMS Microbiol. Rev.19:85–116 [PubMed] [Google Scholar]

2. Perrenoud A, Sauer U. 2005. Impact of global transcriptional regulation by ArcA, ArcB, Cra, Crp, Cya, Fnr, and Mlc on glucose catabolism in Escherichia coli. J Bacteriol187:3171–3179 [PMC free article] [PubMed] [Google Scholar]

3. Gerosa L, Sauer U. Regulation and control of metabolic fluxes in microbes. Curr. Opin. Biotechnol.22:566–575 [PubMed] [Google Scholar]

4. Görke B, Vogel J. 2008. Noncoding RNA control of the making and breaking of sugars. Genes Dev.22:2914–2925 [PubMed] [Google Scholar]

5. Saier MH, Jr, Chauvaux S, Deutscher J, Reizer J, Ye JJ. 1995. Protein phosphorylation and regulation of carbon metabolism in Gram-negative versus Gram-positive bacteria. Trends Biochem. Sci.20:267–271 [PubMed] [Google Scholar]

6. Stock JB, Ninfa AJ, Stock AM. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev.53:450–490 [PMC free article] [PubMed] [Google Scholar]

7. Deutscher J, Francke C, Postma PW. 2006. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev.70:939–1031 [PMC free article] [PubMed] [Google Scholar]

8. Postma PW, Lengeler JW, Jacobson GR. 1993. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev.57:543–594 [PMC free article] [PubMed] [Google Scholar]

9. Saier MH, Jr, Reizer J. 1994. The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol.13:755–764 [PubMed] [Google Scholar]

10. Tchieu JH, Norris V, Edwards JS, Saier MH., Jr 2001. The complete phosphotransferase system in Escherichia coli. J. Mol. Microbiol. Biotechnol.3:329–346 [PubMed] [Google Scholar]

11. Barabote RD, Saier MH., Jr 2005. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol. Mol. Biol. Rev.69:608–634 [PMC free article] [PubMed] [Google Scholar]

12. Reizer J, Reizer A, Saier MH, Jr, Jacobson GR. 1992. A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria. Protein Sci.1:722–726 [PMC free article] [PubMed] [Google Scholar]

13. Pflüger-Grau K, Görke B. 2010. Regulatory roles of the bacterial nitrogen-related phosphotransferase system. Trends Microbiol.18:205–214 [PubMed] [Google Scholar]

14. Lee CR, Cho SH, Yoon MJ, Peterkofsky A, Seok YJ. 2007. Escherichia coli enzyme IIANtr regulates the K+ transporter TrkA. Proc. Natl. Acad. Sci. U. S. A.104:4124–4129 [PMC free article] [PubMed] [Google Scholar]

15. Powell BS, et al. 1995. Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant. J. Biol. Chem.270:4822–4839 [PubMed] [Google Scholar]

16. Cases I, Pérez-Martín J, de Lorenzo V. 1999. The IIANtr (PtsN) protein of Pseudomonas putida mediates the C source inhibition of the sigma54-dependent Pu promoter of the TOL plasmid. J. Biol. Chem.274:15562–15568 [PubMed] [Google Scholar]

17. Cases I, Lopez JA, Albar JP, de Lorenzo V. 2001. Evidence of multiple regulatory functions for the PtsN (IIA(Ntr)) protein of Pseudomonas putida. J. Bacteriol.183:1032–1037 [PMC free article] [PubMed] [Google Scholar]

18. Lüttmann D, et al. 2009. Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIA(Ntr) in Escherichia coli. Mol. Microbiol.72:978–994 [PubMed] [Google Scholar]

19. Velázquez F, Pflüger K, Cases I, De Eugenio LI, de Lorenzo V. 2007. The phosphotransferase system formed by PtsP, PtsO, and PtsN proteins controls production of polyhydroxyalkanoates in Pseudomonas putida. J. Bacteriol.189:4529–4533 [PMC free article] [PubMed] [Google Scholar]

20. Cases I, Velázquez F, de Lorenzo V. 2007. The ancestral role of the phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) as exposed by comparative genomics. Res. Microbiol.158:666–670 [PubMed] [Google Scholar]

21. Pflüger K, de Lorenzo V. 2008. Evidence of in vivo cross talk between the nitrogen-related and fructose-related branches of the carbohydrate phosphotransferase system of Pseudomonas putida. J. Bacteriol.190:3374–3380 [PMC free article] [PubMed] [Google Scholar]

22. Zimmer B, Hillmann A, Görke B. 2008. Requirements for the phosphorylation of the Escherichia coli EIIANtr protein in vivo. FEMS Microbiol. Lett.286:96–102 [PubMed] [Google Scholar]

23. Velázquez F, di Bartolo I, de Lorenzo V. 2004. Genetic evidence that catabolites of the Entner-Doudoroff pathway signal C source repression of the sigma54 Pu promoter of Pseudomonas putida. J. Bacteriol.186:8267–8275 [PMC free article] [PubMed] [Google Scholar]

24. del Castillo T, et al. 2007. Convergent peripheral pathways catalyze initial glucose catabolism in Pseudomonas putida: genomic and flux analysis. J. Bacteriol.189:5142–5152 [PMC free article] [PubMed] [Google Scholar]

25. Fuhrer T, Fischer E, Sauer U. 2005. Experimental identification and quantification of glucose metabolism in seven bacterial species. J. Bacteriol.187:1581–1590 [PMC free article] [PubMed] [Google Scholar]

26. Nogales J, Palssøn BO, Thiele I. 2008. A genome-scale metabolic reconstruction of Pseudomonas putida KT2440: iJN746 as a cell factory. BMC Syst. Biol.2:79. [PMC free article] [PubMed] [Google Scholar]

27. Puchalka J, et al. 2008. Genome-scale reconstruction and analysis of the Pseudomonas putida KT2440 metabolic network facilitates applications in biotechnology. PLoS Comput. Biol.4:e1000210. [PMC free article] [PubMed] [Google Scholar]

28. Van Dijken JP, Quayle JR. 1977. Fructose metabolism in four Pseudomonas species. Arch. Microbiol.114:281–286 [PubMed] [Google Scholar]

29. Sauer U, Eikmanns BJ. 2005. The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria. FEMS Microbiol. Rev.29:765–794 [PubMed] [Google Scholar]

30. Grüning NM, Lehrach H, Ralser M. 2010. Regulatory crosstalk of the metabolic network. Trends Biochem. Sci.35:220–227 [PubMed] [Google Scholar]

31. Pflüger K, de Lorenzo V. 2007. Growth-dependent phosphorylation of the PtsN (EIINtr) protein of Pseudomonas putida. J. Biol. Chem.282:18206–18211 [PubMed] [Google Scholar]

32. Eyzaguirre J, Cornwell E, Borie G, Ramírez B. 1973. Two malic enzymes in Pseudomonas aeruginosa. J. Bacteriol.116:215–221 [PMC free article] [PubMed] [Google Scholar]

33. Choi J, et al. 2010. Salmonella pathogenicity island 2 expression negatively controlled by EIIANtr-SsrB interaction is required for Salmonella virulence. Proc. Natl. Acad. Sci. U. S. A.107:20506–20511 [PMC free article] [PubMed] [Google Scholar]

34. Pflüger-Grau K, Chavarría M, de Lorenzo V. 2011. The interplay of the EIIA(Ntr) component of the nitrogen-related phosphotransferase system (PTS(Ntr)) of Pseudomonas putida with pyruvate dehydrogenase. Biochim. Biophys. Acta1810:995–1005 [PubMed] [Google Scholar]

35. Lee CR, et al. 2005. Requirement of the dephospho-form of enzyme IIANtr for derepression of Escherichia coli K-12 ilvBN expression. Mol. Microbiol.58:334–344 [PubMed] [Google Scholar]

36. Begley GS, Jacobson GR. 1994. Overexpression, phosphorylation, and growth effects of ORF162, a Klebsiella pneumoniae protein that is encoded by a gene linked to rpoN, the gene encoding sigma 54. FEMS Microbiol. Lett.119:389–394 [PubMed] [Google Scholar]

37. Silva-Rocha R, de Lorenzo V. 2010. Noise and robustness in prokaryotic regulatory networks. Annu. Rev. Microbiol.64:257–275 [PubMed] [Google Scholar]

38. Chavarría M, et al. 2011. Fructose 1-phosphate is the preferred effector of the metabolic regulator cra of Pseudomonas putida. J. Biol. Chem.286:9351–9359 [PMC free article] [PubMed] [Google Scholar]

39. Camilli A, Bassler BL. 2006. Bacterial small-molecule signaling pathways. Science311:1113–1116 [PMC free article] [PubMed] [Google Scholar]

40. Commichau FM, Forchhammer K, Stülke J. 2006. Regulatory links between carbon and nitrogen metabolism. Curr. Opin. Microbiol.9:167–172 [PubMed] [Google Scholar]

41. Conway T. 1992. The Entner-Doudoroff pathway: history, physiology and molecular biology. FEMS Microbiol. Rev.9:1–27 [PubMed] [Google Scholar]

42. Diesterhaft MD, Freese E. 1973. Role of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and malic enzyme during growth and sporulation of Bacillus subtilis. J. Biol. Chem.248:6062–6070 [PubMed] [Google Scholar]

43. Portais JC, Delort AM. 2002. Carbohydrate cycling in micro-organisms: what can 13C-NMR tell us?FEMS Microbiol. Rev.26:375–402 [PubMed] [Google Scholar]

44. Fernández S, de Lorenzo V, Pérez-Martín J. 1995. Activation of the transcriptional regulator XylR of Pseudomonas putida by release of repression between functional domains. Mol. Microbiol.16:205–213 [PubMed] [Google Scholar]

45. Cases I, Velázquez F, de Lorenzo V. 2001. Role of ptsO in carbon-mediated inhibition of the Pu promoter belonging to the pWW0 Pseudomonas putida plasmid. J. Bacteriol.183:5128–5133 [PMC free article] [PubMed] [Google Scholar]

46. Miller JH. 1972. Experiments in molecular genetics. Cold Spring Harbor, New York, NY. [Google Scholar]

47. Sauer U, et al. 1999. Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism. J. Bacteriol.181:6679–6688 [PMC free article] [PubMed] [Google Scholar]

48. Dauner M, Sauer U. 2000. GC-MS analysis of amino acids rapidly provides rich information for isotopomer balancing. Biotechnol. Prog.16:642–649 [PubMed] [Google Scholar]

49. Fischer E, Sauer U. 2003. Metabolic flux profiling of Escherichia coli mutants in central carbon metabolism using GC-MS. Eur. J. BioChem.270:880–891 [PubMed] [Google Scholar]

50. Zamboni N, Fischer E, Sauer U. 2005. FiatFlux—a software for metabolic flux analysis from 13C-glucose experiments. BMC Bioinformatics.6:209 [PMC free article] [PubMed] [Google Scholar]

51. Lessie TG, Phibbs PV., Jr 1984. Alternative pathways of carbohydrate utilization in pseudomonads. Annu. Rev. Microbiol.38:359–388 [PubMed] [Google Scholar]

52. Schleissner C, Reglero A, Luengo JM. 1997. Catabolism of D-glucose by Pseudomonas putida U occurs via extracellular transformation into D-gluconic acid and induction of a specific gluconate transport system. Microbiology143:1595–1603 [PubMed] [Google Scholar]

53. Sawyer MH, et al. 1977. Pathways of D-fructose catabolism in species of Pseudomonas. Arch. Microbiol.112:49–55 [PubMed] [Google Scholar]

54. Vicente M, Cánovas JL. 1973. Glucolysis in Pseudomonas putida: physiological role of alternative routes from the analysis of defective mutants. J. Bacteriol.116:908–914 [PMC free article] [PubMed] [Google Scholar]

55. Vicente M. 1975. The uptake of fructose by Pseudomonas putida. Arch. Microbiol.102:163–166 [PubMed] [Google Scholar]

56. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. BioChem.72:248–254 [PubMed] [Google Scholar]

57. Geer BW, Krochko D, Williamson JH. 1979. Ontogeny, cell distribution, and the physiological role of NADP-malic enxyme in Drosophila melanogaster. Biochem. Genet.17:867–879 [PubMed] [Google Scholar]

58. Warren GB, Tipton KF. 1974. Pig liver pyruvate carboxylase. The reaction pathway for the decarboxylation of oxaloacetate. Biochem. J.139:321–329 [PMC free article] [PubMed] [Google Scholar]

Источник: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3312210/
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Similar-sized protein separation

MIL-100(Cr) PE MMM-86% membrane was mounted a dead-end filtration cell. First, 3.3 mg of BSA (66 kDa) and 3.3 mg of BHb (65 kDa) were dissolved into the 10 mL of deionized water. Then, 1 mL of mixture was taken from initial solution and re-dispersed into 9 mL of buffer solution at pH = 4.7 (total concentration = 0.066 mg mL−1). The separation time was varied from 1 to 5 h with 1 h of the interval. Collected samples at 1–5 h were dried in 70 °C vacuum oven and re-dispersed in the excessive amount of buffer (2 mL).