The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31

Biochimie

Volumn 91, Issue 11-12, 2009, Pages 1434-1442

  Kang, Min Sun ^a   Okuyama, Masayuki ^a   Mori, Haruhide ^a   Kimura, Atsuo ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

1,3 Glucosidase; Glycoside hydrolase family 31; Inclusion body formation; Lactobacillus johnsonii

Indexed keywords

ALPHA 1,3 GLUCOSIDASE; ALPHA GLUCOSIDASE; BENZYL ALCOHOL; CHAPERONE; CHAPERONIN; DISACCHARIDE; GLYCOSIDASE; PREBIOTIC AGENT; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ACREMONIUM; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CELL INCLUSION; CONTROLLED STUDY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE EXPRESSION SYSTEM; GENE OVEREXPRESSION; GENETIC CONSERVATION; GENOME ANALYSIS; GLYCOSYLATION; HYDROLYSIS; LACTOBACILLUS JOHNSONII; MOLECULAR CLONING; MOULD; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN INDUCTION; SEQUENCE HOMOLOGY;

ALPHA-GLUCOSIDASES; CLONING, MOLECULAR; DISACCHARIDES; DNA, BACTERIAL; ESCHERICHIA COLI; GLYCOSIDE HYDROLASES; MOLECULAR SEQUENCE DATA; POTASSIUM CHANNELS, INWARDLY RECTIFYING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; YEASTS;

ACREMONIUM IMPLICATUM; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; LACTOBACILLUS JOHNSONII;

EID: 72649094480     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.07.018     Document Type: Article

References (64)

1. Link-Amster H., Rochat F., Saudan K.Y., Mignot O., and Aeschlimann J.M. Modulation of a specific humoral immune response and changes in intestinal flora mediated through fermented milk intake. FEMS Immunol. Med. Microbiol. 63 (1994) 2747-2753
2. Kaburagi T., Yamano T., Fukushima Y., Yoshino H., Mito N., and Sato K. Effect of Lactobacillus johnsonii La1 on immune function and serum albumin in aged and malnourished aged mice. Nutrition 23 (2007) 342-350
3. Marteau P., Vaerman J.P., Dehennin J.P., et al. Effects of intrajejunal perfusion and chronic ingestion of Lactobacillus johnsonii strain La1 on serum concentrations and jejunal secretions of immunoglobulins and serum proteins in healthy humans. Gastroenterol. Clin. Biol. 21 (1997) 293-298
4. Schiffrin E.J., Rochat F., Link-Amster H., Aeschlimann J.M., and Donnet-Hughes A. Immunomodulation of human blood cells following the ingestion of lactic acid bacteria. J. Dairy Sci. 78 (1995) 491-497
5. Bernet M.F., Brassart D., Neeser J.R., and Servin A.L. Lactobacillus acidophilus La1 binds to cultured human intestinal cell lines and inhibits cell attachment and cell invasion by enterovirulent bacteria. Gut 35 (1994) 483-489
6. La Ragione R.M., Narbad A., Gasson M.J., and Woodward M.J. In vivo characterization of Lactobacillus johnsonii FI9785 for use as a defined competitive exclusion agent against bacterial pathogens in poultry. Lett. Appl. Microbiol. 38 (2004) 197-205
7. Gotteland M., and Cruchet S. Suppressive effect of frequent ingestion of Lactobacillus johnsonii La1 on Helicobacter pylori colonization in asymptomatic volunteers. J. Antimicrob. Chemother. 51 (2003) 1317-1319
8. Michetti P., Dorta G., Wiesel P.H., et al. Effect of whey-based culture supernatant of Lactobacillus acidophilus (johnsonii) La1 on Helicobacter pylori infection in humans. Digestion 60 (1999) 203-209
9. Sgouras D.N., Panayotopoulou E.G., Martinez-Gonzalez B., Petraki K., Michopoulos S., and Mentis A. Lactobacillus johnsonii La1 attenuates Helicobacter pylori-associated gastritis and reduces levels of proinflammatory chemokines in C57BL/6 mice. Clin. Diagn. Lab. Immunol. 12 (2005) 1378-1386
10. Pridmore R.D., Berger B., Desiere F., et al. The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2512-2517
11. Denou E., Berger B., Barretto C., Panoff J.M., Arigoni F., and Brüssow H. Gene expression of commensal Lactobacillus johnsonii strain NCC533 during in vitro growth and in the murine gut. J. Bacteriol. 189 (2007) 8109-8119
12. Denou E., Pridmore R.D., Berger B., Panoff J.M., Arigoni F., and Brüssow H. Identification of genes associated with the long-gut-persistence phenotype of the probiotic Lactobacillus johnsonii strain NCC533 using a combination of genomics and transcriptome analysis. J. Bacteriol. 190 (2008) 3161-3168
13. Macfarlane S., Macfarlane G.T., and Cummings J.H. Review article: prebiotics in the gastrointestinal tract. Aliment. Pharmacol. Ther. 24 (2006) 701-714
14. Haase-Pettingell C.A., and King J. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation. J. Biol. Chem. 263 (1988) 4977-4983
15. Mitraki A., and King J. Protein folding intermediates and inclusion body formation. Nat. Biotechnol. 7 (1989) 690-697
16. Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
17. LaVallie E.R., DiBlasio E.A., Kovacic S., Grant K.L., Schendel P.F., and McCoy J.M. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Nat. Biotechnol. 11 (1993) 187-193
18. Roodveldt C., Aharoni A., and Tawfik D.S. Directed evolution of proteins for heterologous expression and stability. Curr. Opin. Struct. Biol. 15 (2005) 50-56
19. Lin K., Kurland I., Xu L.Z., et al. Expression of mammalian liver glycolytic/gluconeogenic enzymes in Escherichia coli: recovery of active enzyme is strain and temperature dependent. Protein Expr. Purif. 1 (1990) 169-176
20. Yang Q.H., Wu C.L., Lin K., and Li L. Low concentration of inducer favors production of active form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli. Protein Expr. Purif. 10 (1997) 320-324
21. Georgiou G., and Valax P. Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotechnol. 7 (1996) 190-197
22. Kiefhaber T., Rudolph R., Kohle H.H., and Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Nat. Biotechnol. 9 (1991) 825-829
23. Jacob M., Schindler T., Balbach J., and Schmid F.X. Diffusion control in an elementary protein folding reaction. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 5622-5627
24. Yang D.S., Yip C.M., Huang T.H., Chakrabartty A., and Fraser P.E. Manipulating the amyloid-β aggregation pathway with chemical chaperones. J. Biol. Chem. 274 (1999) 32970-32974
25. Russo A.T., Rösgen J., and Bolen D.W. Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization. J. Mol. Biol. 330 (2003) 851-866
26. Blackwell J.R., and Horgan R. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett. 295 (1991) 10-12
27. de Marco A., Vigh L., Diamant S., and Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones 10 (2005) 329-339
28. Oganesyan N., Ankoudinova I., Kim S.H., and Kim R. Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization. Protein Expr. Purif. 52 (2007) 280-285
29. Becker J., and Craig E.A. Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219 (1994) 11-23
30. Feder M.E., and Hofmann G.E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 61 (1999) 243-282
31. Fayet O., Ziegelhoffer T., and Georgopoulos C. The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171 (1989) 1379-1385
32. Horwich A.L., Low K.B., Fenton W.A., Hirshfield N.I., and Furtak K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74 (1993) 909-917
33. Houry W.A., Frishman D., Eckerskorn C., Lottspeich F., and Hartl F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature 402 (1999) 147-154
34. Horváth I., Glatz A., Varvasovszki V., et al. Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene". Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 3513-3518
35. Nagy E., Balogi Z., Gombos I., et al. Hyperfluidization-coupled membrane microdomain reorganization is linked to activation of the heat shock response in a murine melanoma cell line. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 7945-7950
36. Rice P., Longden I., and Bleasby A. EMBOSS: the European molecular biology open software suite. Trends Genet. 16 (2000) 276-277
37. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: signalP 3.0. J. Mol. Biol. 340 (2004) 783-795
38. Pearson W.R. Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 183 (1990) 63-98
39. Bairoch A., and Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res. 27 (1999) 49-54
40. Thompson J.D., Higgins D.G., and Gibson T.J. 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 (1994) 4673-4680
41. Larkin M.A., Blackshields G., Brown N.P., et al. Clustal W and Clustal X version 2.0. Bioinformatics 23 (2007) 2947-2948
42. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
43. Miwa I., Okudo J., Maeda K., and Okuda G. Mutarotase effect on colorimetric determination of blood glucose with β-d-glucose oxidase. Clin. Chim. Acta 37 (1972) 538-540
44. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
45. Matsui H., Sasaki M., Takemasa E., Kaneta T., and Chiba S. Kinetic studies on the substrate specificity and active site of rabbit muscle acid α-glucosidase. J. Biochem. 96 (1984) 993-1004
46. Suzuki Y., Nobiki M., Matsuda M., and Sawai T. Bacillus thermoamyloliquefaciens KP1071 α-glucosidase II is a thermostable Mr 540,000 homohexameric α-glucosidase with both exo-α-1,4-glucosidase and oligo-1,6-glucosidase activities. Eur. J. Biochem. 245 (1997) 129-136
47. Trombetta E.S., Simons J.F., and Helenius A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271 (1996) 27509-27516
48. Pelletier M.F., Marcil A., Sevigny G., et al. The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 10 (2000) 815-827
49. Trombetta E.S., Fleming K.G., and Helenius A. Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry 40 (2001) 10717-10722
50. Kerner M.J., Naylor D.J., Ishihama Y., et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122 (2005) 209-220
51. Lovering A.L., Lee S.S., Kim Y.W., Withers S.G., and Strynadka N.C. Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem. 280 (2005) 2105-2115
52. Ernst H.A., Lo Leggio L., Willemoës M., Leonard G., Blum P., and Larsen S. Structure of the Sulfolobus solfataricus α-glucosidase: implications for domain conservation and substrate recognition in GH31. J. Mol. Biol. 358 (2006) 1106-1124
53. Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., and Hartl F.U. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352 (1991) 36-42
54. Leskelä S., Kontinen V.P., and Sarvas M. Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence. Microbiology 142 (1996) 71-77
55. Hüwel S., Haalck L., Conrath N., and Spener F. Production and stabilization of pure maltose phosphorylase from Lactobacillus brevis for sensing inorganic phosphate. Ann. N.Y. Acad. Sci. 799 (1996) 701-706
56. Watanabe K., Chishiro K., Kitamura K., and Suzuki Y. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266 (1991) 24287-24294
57. Davies G.J., Wilson K.S., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321 (1997) 557-559
58. Yamamoto T., Unno T., Watanabe Y., Yamamoto M., Okuyama M., Mori H., Chiba S., and Kimura A. Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage. Biochim. Biophys. Acta 1700 (2004) 189-198
59. Torre-Bouscoulet M.E., López-Romero E., Balcázar-Orozco R., Calvo-Méndez C., and Flores-Carreón A. Partial purification and biochemical characterization of a soluble α-glucosidase II-like activity from Candida albicans. FEMS Microbiol. Lett. 236 (2004) 123-128
60. Grinna L.S., and Robbins P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814-8818
61. Grinna L.S., and Robbins P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255-2258
62. Murosaki S., Muroyama K., Yamamoto Y., Kusaka H., Liu T., and Yoshikai Y. Immunopotentiating activity of nigerooligosaccharides for the T helper 1-like immune response in mice. Biosci. Biotechnol. Biochem. 63 (1999) 373-378
63. Murosaki S., Muroyama K., Yamamoto Y., Liu T., and Yoshikai Y. Nigerooligosaccharides augments natural killer activity of hepatic mononuclear cells in mice. Int. Immunopharmacol. 2 (2002) 151-159
64. Tuohy K.M., Rouzaud G.C., Brück W.M., and Gibson G.R. Modulation of the human gut microflora towards improved health using prebiotics - assessment of efficacy. Curr. Pharm. Des. 11 (2005) 75-90