A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica has specificity for the 5-phosphate of myo-inositol hexakisphosphate

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 10, 2008, Pages 2053-2064

  Puhl, Aaron A ^a   Greiner, Ralf ^b   Selinger, L Brent ^a  

^a UNIVERSITY OF LETHBRIDGE   (Canada)

^b FEDERAL RESEARCH INSTITUTE OF NUTRITION AND FOOD   (Germany)

Author keywords

Hydrolysis pathway; Inositol polyphosphate phosphatase; myo Inositol; Phytase; Protein tyrosine phosphatase

Indexed keywords

DNA FRAGMENT; PHYTATE; PROTEIN TYROSINE PHOSPHATASE; RECOMBINANT DNA; RECOMBINANT RNA; TYROSINE PHOSPHATASE LIKE INOSITOL POLYPHOSPHATASE;

AMINO ACID SEQUENCE; ARTICLE; BIOINFORMATICS; DNA ISOLATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; GENE EXPRESSION; GENETIC CODE; HIGH ENERGY PHOSPHATE; HUMAN; HYDROLYSIS; ION PAIR CHROMATOGRAPHY; METABOLISM; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PROTEIN DEPHOSPHORYLATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SELENOMONAS RUMINANTIUM; SELENOMONAS RUMINANTIUM SUBSPECIE LACTILYTICA;

6-PHYTASE; AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CLONING, MOLECULAR; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; OSMOLAR CONCENTRATION; PHOSPHATES; PHOSPHORYLATION; PHYTIC ACID; PROTEIN TYROSINE PHOSPHATASES; RECOMBINANT PROTEINS; SELENOMONAS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA; SELENOMONAS RUMINANTIUM;

EID: 48949117581     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.02.003     Document Type: Article

References (67)

1. Allen S.D., Emery C.L., and Lyerly D.M. Clostridium. In: Murray P.R., Baron E.J., Jorgensen J.H., Pfaller M.A., and Yolken R.H. (Eds). Manual of clinical microbiology (2003), ASM Press, Washington 835-856
2. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tool. Journal of Molecular Biology 215 (1990) 403-410
3. Baldi P., and Pollastri G. The principled design of large-scale recursive neural network architectures-DAG-RNNs and the protein structure prediction problem. Journal of Machine Learning Research 4 (2003) 575-603
4. Barker C.J., French P.J., Moore A.J., Nilsson T., Berggren P.O., Bunce C.M., et al. Inositol 1,2,3-trisphosphate and inositol 1,2-bisphosphate and/or 2,3-bisphosphate are normal constituents of mammalian-cells. Biochemical Journal 306 (1995) 557-564
5. Barrientos L., Scott J.J., and Murthy P.P.N. Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen. Plant Physiology 106 (1994) 1489-1495
6. Bendtsen J.D., Nielson H., Von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. Journal of Molecular Biology 340 (2004) 783-795
7. Bennett M., Onnebo S.M.N., Azevedo C., and Saiardi A. Inositol pyrophosphates: Metabolism and signaling. Cellular and Molecular Life Sciences 63 (2006) 552-564
8. Benson D.A., Karsch-Mizrachi I., Lipman D.J., Ostell J., and Wheeler D.L. GenBank. Nucleic Acids Research 34 (2006) D16-D20
9. Bliska J., Guan K., Dixon J., and Falkow S. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proceedings of the National Academy of Sciences USA 88 (1991) 1187-1191
10. Brailoiu E., Miyamoto M.D., and Dun N.J. Inositol derivatives modulate spontaneous transmitter release at the frog neuromuscular junction. Neuropharmacology 45 (2003) 691-701
11. Bretz J.R., Mock N.M., Charity J.C., Zeyad S., Baker C.J., and Hutcheson S.W. A translocated protein tyrosine phosphatase of Pseudomonas syringae pv. tomato DC3000 modulates plant defence response to infection. Molecular Microbiology 49 (2003) 389-400
12. Caldwell D.R., and Bryant M.P. Medium without rumen fluid for nonselective enumeration and isolation of rumen bacteria. Applied Microbiology 14 (1966) 794-801
13. Chen P., and Lott J.N.A. Studies of Capsicum annuum seeds: Structure, storage reserves, and mineral nutrients. Canadian Journal of Botany 70 (1992) 518-529
14. Cheng J., Randall A.Z., Sweredoski M.J., and Baldi P. SCRATCH: A protein structure and structural feature prediction server. Nucleic Acids Research 33 (2005) W72-W76
15. Chenna R., Sugawara H., Koike T., Lopez R., Gibson T.J., Higgins D.G., et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Research 31 (2003) 3497-3500
16. Chi T.H., and Crabtree G.R. Inositol phosphates in the nucleus. Science 287 (2000) 1937-1938
17. Chu H.M., Guo R.T., Lin T.W., Chou C.C., Shr H.L., Lai H.L., et al. Structures of Selenomonas ruminantium phytase in complex with persulfated phytate: DSP phytase fold and mechanism for sequential substrate hydrolysis. Structure 12 (2004) 2015-2024
18. Collingro A., Toenshoff E.R., Taylor M.W., Fritsche T.R., Wagner M., and Horn M. 'Candidatus Protochlamydia amoebophila', an endosymbiont of Acanthamoeba spp. International Journal of Systematic and Evolutionary Microbiology 55 (2005) 1863-1866
19. D'Silva C.G., Bae H.D., Yanke L.J., Cheng K.J., and Selinger L.B. Localization of phytase in Selenomonas ruminantium and Mitsuokella multiacidus by transmission electron microscopy. Canadian Journal of Microbiology 46 (2000) 391-395
20. Espinosa A., Guo M., Tam V.C., Fu Z.Q., and Alfano J.R. The Pseudomonas syringae type III-secreted protein HopPtoD2 possesses protein tyrosine phosphatase activity and suppresses programmed cell death in plants. Molecular Microbiology 49 (2003) 377-387
21. Fassler J., Nadel C., Richardson N., McEntyre J., Schuler G., McGinnis S., et al. NCBI website (2000), National Center for Biotechnology Information. National Library of Medicine. National Institutes of Health, Bethesda, MD
22. Fu Y., and Galan J.E. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Molecular Microbiology 27 (1998) 359-368
23. Gaidarov I., Smith M.E., Domin J., and Keen J.H. The class II phosphoinositide 3-kinase C2 alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking. Molecular Cell 7 (2001) 443-449
24. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., et al. Protein identification and analysis tools on the ExPASy server. In: Walker J.M. (Ed). The proteomics protocols handbook (2005), Humana Press 571-607
25. Greer J. Comparative model-building of the mammalian serine proteases. Journal of Molecular Biology 153 (1981) 1027-1042
26. Greiner R., Alminger M.L., Carlsson N.G., Muzquiz M., Burbano C., Cuadrado C., et al. Pathway of dephosphorylation of myo-inositol hexakisphosphate by phytases of legume seeds. Journal of Agricultural and Food Chemistry 50 (2002) 6865-6870
27. Greiner R., Farouk A., Alminger M.L., and Carlsson N.G. The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytate-degrading enzymes of different Bacillus spp. Canadian Journal of Microbiology 48 (2002) 986-994
28. Greiner R., Haller E., Konietzny U., and Jany K.D. Purification and characterization of a phytase from Klebsiella terrigena. Archives of Biochemistry and Biophysics 341 (1997) 201-206
29. Greiner R., Lim B., Cheng C., and Carlsson N.-G. Pathway of phytate dephosphorylation by β-propeller phytases of different origins. Canadian Journal of Microbiology 53 (2007) 488-495
30. Hanakahi L.A., Bartlet-Jones M., Chappell C., Pappin D., and West S.C. Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair. Cell 102 (2000) 721-729
31. Hartman G.L., and Yang C.H. Occurrence of three races of Xanthomonas campestris pv. vesicatoria on pepper and tomato in Taiwan. Plant Disease 74 (1990) 252
32. Hawkins P.T., Poyner D.R., Jackson T.R., Letcher A.J., Lander D.A., and Irvine R.F. Inhibition of iron-catalyzed hydroxyl radical formation by inositol polyphosphates - a possible physiological function for myo-inositol hexakisphosphate. Biochemical Journal 294 (1993) 929-934
33. Heinonen J.K., and Lahti R.J. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Analytical Biochemistry 113 (1981) 313-317
34. Higgins D., Thompson J., and Gibson T. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22 (1994) 4673-4680
35. Irvine R.F. Inositide evolution-towards turtle domination?. The Journal of Physiology 566 (2005) 295-300
36. Kennelly P.J., and Potts M. Life among the primitives: Protein o-phosphatases in prokaryotes. Frontiers in Bioscience 4 (1999) d372-d385
37. Kim H.W., Kim Y.O., Lee J.H., Kim K.K., and Kim Y.J. Isolation and characterization of a phytase with improved properties from Citrobacter braakii. Biotechnology Letters 25 (2003) 1231-1234
38. Konietzny U., and Greiner R. Molecular and catalytic properties of phytate-degrading enzymes (phytases). International Journal of Food Science and Technology 37 (2002) 791-812
39. Kurimoto T., Tachibana C., Suzuki M., and Watanabe T. Biological and chemical characterization of lipopolysaccharide from Selenomonas spp. in human periodontal pockets. Infection and Immunity 51 (1986) 969-971
40. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
41. Loewus F.A., and Murthy P.P.N. Myo-inositol metabolism in plants. Plant Science 150 (2000) 1-19
42. Lott J.N.A., and Buttrose M.S. Location of reserves of mineral elements in seed protein bodies: Macadamia nut, walnut and hazel nut. Canadian Journal of Botany 56 (1978) 2072-2082
43. Mandel N.C., Burman S., and Biswas B.B. Isolation, purification and characterization of phytase from germinating mung beans. Phytochemistry 11 (1972) 495-502
44. Mehta B.D., Joga S.P., Johnson S.C., and Murthy P.P.N. Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP). Phytochemistry 67 (2006) 1874-1886
45. Mullaney E.J., and Ullah A.H.J. The term phytase comprises several different classes of enzymes. Biochemical and Biophysical Research Communications 312 (2003) 179-184
46. Nakashima B.A., McAllister T.A., Sharma R., and Selinger L.B. Diversity of phytases in the rumen. Microbial Ecology 53 (2006) 82-88
47. Nicholas, K. B., Jr., Nicholas, H. B., & Deerfield D. W., I. (1997). GeneDoc: Analysis and visualization of genetic variation. EMBNEW.NEWS 4:14.
48. Nielsen H., Engelbrecht J., Brunak S., and Von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering 10 (1997) 1-6
49. Orchiston E.A., Bennett D., Leslie N.R., Clarke R.G., Winward L., Downes C.P., et al. PTEN M-CBR3, a versatile and selective regulator of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P-5)-Evidence for Ins(1,3,4,5,6)P-5 as a proliferative signal. Journal of Biological Chemistry 279 (2004) 1116-1122
50. Phillippy B.Q., and Bland J.M. Gradient ion chromatography of inositol phosphates. Analytical Biochemistry 175 (1988) 162-166
51. Phillipy B.Q., and Graf E. Antioxidant functions of inositol 1,2,3-trisphosphate and inositol 1,2,3,6-tetrakisphosphate. Free Radical Biology and Medicine 22 (1997) 939-946
52. Pollastri G., Przybylski D., Rost B., and Baldi P. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 47 (2002) 228-235
53. Priefer U., Simon R., and Pühler A. Cloning with cosmids. In: Pühler A., and Timmis K.N. (Eds). Advanced molecular genetics (1984), Springer-Verlag NY, New York 190-201
54. Puhl A.A., Gruninger R.J., Greiner R., Janzen T.W., Mosimann S.C., and Selinger B.L. Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase. Protein Science 16 (2007) 1368-1378
55. Raboy V. Myo-Inositol-1,2,3,4,5,6-hexakisphosphate. Phytochemistry 64 (2003) 1033-1043
56. Sasakawa N., Sharif M., and Hanley M.R. Metabolism and biological-activities of inositol pentakisphosphate and inositol hexakisphosphate. Biochemical Pharmacology 50 (1995) 137-146
57. Scott H.W., and Dehority B.A. Vitamin requirements of several cellulolytic bacteria. Journal of Bacteriology 89 (1965) 1169-1175
58. Shears S.B. Assessing the omnipotence of inositol hexakisphosphate. Cellular Signalling 13 (2001) 151-158
59. Shi L., Potts M., and Kennelly P.J. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait. FEMS Microbiology Reviews 22 (1998) 229-253
60. Shuman H.A., Purcell M., Segal G., Hales L., and Wiater L.A. Intracellular multiplication of Legionella pneumophila: Human pathogen or accidental tourist?. Current Topics in Microbiology and Immunology 225 (1998) 99-112
61. Skoglund E., Carlsson N.G., and Sandberg A.S. High-performance chromatographic separation of inositol phosphate isomers on strong anion exchange columns. Journal of Agricultural and Food Chemistry 46 (1998) 1877-1882
62. Smith A.W., Poyner D.R., Hughes H.K., and Lambert P.A. Siderophore activity of myoinositol hexakisphosphate in Pseudomonas-aeruginosa. Journal of Bacteriology 176 (1994) 3455-3459
63. Vanhartingsveldt W., Vanzeijl C.M.J., Harteveld G.M., Gouka R.J., Suykerbuyk M.E.G., Luiten R.G.M., et al. Cloning, characterization and overexpression of the phytase-encoding gene (Phya) of Aspergillus-niger. Gene 127 (1993) 87-94
64. Vohra A., and Satyanarayana T. Phytases: Microbial sources, production, purification, and potential biotechnological applications. Critical Reviews in Biotechnology 23 (2003) 29-60
65. Walcott R.R., Fessehaie A., and Castro A.C. Differences in pathogenicity between two genetically distinct groups of Acidovorax avenae subsp. citrulli on cucurbit hosts. Journal of Phytopathology 152 (2004) 277-285
66. Yanke L.J., Bae H.D., Selinger L.B., and Cheng K.J. Phytase activity of anaerobic ruminal bacteria. Microbiology-Uk 144 (1998) 1565-1573
67. Zhang Z.Y. Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development. Annual Review of Pharmacology and Toxicology 42 (2002) 209-234