Characterization of a bifunctional HPr kinase/phosphorylase from Leuconostoc mesenteroides SY1

Journal of Microbiology and Biotechnology

Volumn 18, Issue 4, 2008, Pages 746-753

  Park, Jae Yong ^a   Lee, Kang Wook ^a   Lee, Ae Ran ^a   Jeong, Woo Ju ^a   Chun, Jiyeon ^b   Lee, Jong Hoon ^c   Kim, Jeong Hwan ^a  

^a Gyeongsang National University   (South Korea)

^b Sunchon National University   (South Korea)

^c Kyonggi University   (South Korea)

Author keywords

Catabolite repression; HPr kinase phosphorylase; hprK; Leuconostoc mesenteroides

Indexed keywords

FRUCTOSE 1,6 BISPHOSPHATE; HPR KINASE; HPR PHOSPHORYLASE; MAGNESIUM ION; MANGANESE; PHOSPHOENOLPYRUVATE; REGULATOR PROTEIN; SERINE; BACTERIAL PROTEIN; PHOSPHORYLASE; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN;

ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIUM ISOLATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; GENE FUNCTION; GENETIC TRANSCRIPTION; LEUCONOSTOC MESENTEROIDES; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN FUNCTION; PROTEIN PURIFICATION; REGULATORY MECHANISM; AMINO ACID SEQUENCE; CHEMISTRY; DNA SEQUENCE; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; KINETICS; LEUCONOSTOC; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; PHOSPHORYLATION; SEQUENCE ALIGNMENT; VEGETABLE;

LEUCONOSTOC MESENTEROIDES;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; KINETICS; LEUCONOSTOC; MOLECULAR SEQUENCE DATA; PHOSPHORYLASES; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; TRANSCRIPTION, GENETIC; VEGETABLES;

EID: 48649101144     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article

References (26)

1. Brochu, D. and C. Vsfrnonvorut. 1999. The HPr(Ser) kinase of Septococcus salivarius: Purification, properties, and cloning of the hprK gene. J. Bacteriol. 181: 709-717.
2. Brückner, R. and F. Titgemeyer. 2002. Carbon catabolite repression in bacteria: Choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol. Lett. 209: 141-148.
3. Deutscher, J., U. Kessler, and W. Hengsternberg. 1985. Streptococcal phosphoenolpyruvate: Sugar phosphotransferase system: Purification and characterization of a phosphoprotein phosphatase which hydrolyzed the phosphoryl bond in serylphosphorylated histidine containing protein. J. Bacteriol. 163: 1203-1209.
4. Deutscher, J., J. Reizer, C. Fischer, A. Galinier, M. H. Saier Jr., and M. Steinmetz. 1994. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J. Bacteriol. 176: 3336-3344.
5. Djordjevic, G. M., J. H. Tchieu, and M. H. Saier Jr. 2004. Genes involved in control of galactose uptake in Lactobacillus brevis and reconstitution of the regulatory system in Bacillus subtilis. J. Bacteriol. 183: 3224-3236.
6. Dossonnet, V., V. Mondero, M. Zagorec, A. Galinier, G. Pérex-Martinez, and J. Deutscher. 2000. Phosphorylation of HPr by the bifunctional HPr kinase/P-ser-HPr phosphorylase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion. J. Bacteriol. 182: 2582-2590.
7. Fieulaine, S., S. Morera, S. Poncet, V. Monedero, V. Gueguen-Chaignon, A. Galinier, J. Janin, J. Deutscher, and S. Nessler. 2001. X-ray structure of HPr kinase: A bacterial protein kinase with a P-loop nucleotide binding domain. EMBO J. 20: 3917-3927.
8. Galinier, A., J. P. Lavergne, C. Geourjon, S. Fieulaine, S. Nessler, and J. M. Jault. 2002. A new family of phosphotransferase with a P-loop motif. J. Biol. Chem. 277: 11362-11367.
9. Gonzalez, C. F., A. J. Stonestrom, G. L. Lorca, and M. H. Saier Jr. 2005. Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases. Biochemistry 44: 598-608.
10. Han, H. U., C. R. Lim, and H. K. Park. 1990. Determination of microbial community as an indicator of kimchi fermentation. Kor. J. Food Sci. Technol. 22: 26-32.
11. Higgins, D., J. Thompson, T. Gibson, J. D. Thompson, D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
12. Hueck, C. J., W. Hillen, and M. H. Saier Jr. 1994. Analysis of a cis-active sequence mediating catabolite repression in Gram-positive bacteria. Res. Microbiol. 145: 503-518.
13. Jeong, S.-J., G. H. Kwon, J. Chun, J. S. Kim, C.-S. Park, D. Y. Kwon, and J. H. Kim. 2007. Cloning of fibrinolytic enzyme gene from Bacillus subtilis isolated from cheonggukjang and its expression in protease-deficient Bacillus subtilis strains. J. Microbiol. Biotechnol. 17: 1018-1023.
14. Kim, J.-H., J.-Y. Park, S.-J. Jeong, J. Chun, and J. H. Kim. 2005. Cold shock response of Leuconotoc mesenteroides SY1 isolated from kimchi. J. Microbiol. Biotechnol. 15: 831-837.
15. Kleerebezem, M., J. Boekhorst, R. van Kranenburg, D. Molenaar, O. P. Kuipers, R. Leer, R. Tarchini, S. A. Peters, H. M. Sandbrink, M. W. Fiers, W. Stickema, R. M. Lankhorst, P. A. Bron, S. M. Hoffer, M. N. Groot R. Kerkhoven, M. de Vries, B. Ursing, W. M. de Vos, and R. J. Siezen. 2003. Complete genome sequence of Lactobacillus plantarum WCFS1. Proc: Natl. Acad. Sci. USA 100: 1990-1995.
16. Lee, K. H., J.-Y. Park S.-J. Jeong, G.-H. Kwon, H.-J. Lee, H. C. Chang, D. K. Chung, J.-H. Lee, and J. H. Kim. 2007. Characterization of paraplantaricin C7, a novel bacteriocin produced by Lactobacillus paraplantarum C7 isolated from kimchi. J. Microbiol. Biotechnol. 17: 287-296.
17. Marquez, J. A., S. Hasenbein, B. Koch, S. Ficulaine, S. Nessler, R. B. Russell, W. Hengstenberg, and K. Scheffzek. 2002. Structure of the full-length HPr kinase/phosphorylase from Staphylococcus xylosus at 1.95 Å resolution; mimicking the product/substrate of the phosphor transfer reactions. Proc. Natl. Acad. Sci. USA 99: 3458-3463.
18. Park, J.-Y., S.-J. Jeong, J. Chun, J.-H. Lee, D. K. Chung, and J. H. Kim. 2006. Characterization of ptsHI operon from Leuconostoc mesenteroides SY1, a strain isolated from kimchi. J. Microbiol. Biotechnol. 16: 988-992.
19. Park, J.-Y., J.-S. Park, J.-H. Kim, S.-J. Jeong, J. Chun, J.-H. Lee, and J. H. Kim. 2005. Characterization of the catabolite control protein (CcpA) gene from Leuconostoc mesenteroides SY1. J. Microbiol. Biotechnol. 15: 749-755.
20. Reizer, J., J. Deutscher, and M. H. Saier Jr. 1998. Metabolite-sensitive, ATP-dependent, protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system in Gram-positive bacteria. Biochemie 71: 989-996.
21. Reizer, J., M. J. Novotny, W. Hengstenberg, and M. H. Saier Jr. 1984. Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system. J. Bacteriol. 160: 333-340.
22. Reizer, J., C. Hoischen, F. Titgemeyer, C. Rivolta, R. Rabus, J. Stülke, D. Karamata, M. H. Saier Jr., and W. Hillen. 1998. A novel protein kinase that controls carbon catabolite repression in bacteria. Mol. Microbiol. 27: 1157-1169.
23. Thevenot, T., D. Brochu, C. Vadeboncoeur, and I. R. Hamilton. 1995. Regulation of ATP-dependent P-(Ser)-HPr formation in Streptococcus mutans and Streptococcus salivarius. J. Bacteriol. 177: 2751-2759.
24. Titgemeyer, F. and W. Hillen. 2002. Global control of sugar metabolism: A Gram-positive solution. Antonie van Leeuwenhoek 82: 59-71.
25. Viana, R., V. Monedero, V. Dossonnet, C. Vadeboncoeur, G. Perez-Martinez, and J. Deutscher. 2000. Enzyme I and HPr from Lactobacillus casei: Their role in sugar transport, carbon catabolite repression and inducer exclusion. Mol. Microbiol. 36: 570-584.
26. Walker, J. E., M. Saraste, J. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the alph- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1: 945-951.