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Volumn 168, Issue 4, 2013, Pages 315-323

E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins

Author keywords

N Acetylglucosaminidase; nagZ; ABL2; CREB1; CXC; D2O; DSS; E. coli; FABD; FITC WGA; Glycosidase; Km; LB; LOQ; MU GlcNAc; MurNAc; NaCl; NagZ; NMR; O GlcNAc; OGA; OGT; PNP GlcNAc; PUGNAc; Q2; S N; SDS PAGE; Tris; UDP GlcNAc

Indexed keywords

ABL2; CREB1; CXC; DSS; E. COLI; FABD; FITC-WGA; GLYCOSIDASES; LB; LOQ; MU-GLCNAC; MURNAC; N-ACETYLGLUCOSAMINIDASE; NACL; NAGZ; O-GLCNAC; OGA; OGT; PNP-GLCNAC; PUGNAC; Q2; SDS-PAGE; TRIS; UDP-GLCNAC;

EID: 84888818868     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.10.008     Document Type: Article
Times cited : (11)

References (45)
  • 3
    • 0025015612 scopus 로고
    • Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase
    • Beer D., Maloisel J.L., Rast D.M., Vasella A. Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase. Helvetica Chimica Acta 1990, 73:1918-1922.
    • (1990) Helvetica Chimica Acta , vol.73 , pp. 1918-1922
    • Beer, D.1    Maloisel, J.L.2    Rast, D.M.3    Vasella, A.4
  • 4
    • 80052466536 scopus 로고    scopus 로고
    • Evidence coupling increased hexosamine biosynthesis pathway activity to membrane cholesterol toxicity and cortical filamentous actin derangement contributing to cellular insulin resistance
    • Bhonagiri P., Pattar G.R., Habegger K.M., McCarthy A.M., Tackett L., Elmendorf J.S. Evidence coupling increased hexosamine biosynthesis pathway activity to membrane cholesterol toxicity and cortical filamentous actin derangement contributing to cellular insulin resistance. Endocrinology 2011, 152:3373-3384.
    • (2011) Endocrinology , vol.152 , pp. 3373-3384
    • Bhonagiri, P.1    Pattar, G.R.2    Habegger, K.M.3    McCarthy, A.M.4    Tackett, L.5    Elmendorf, J.S.6
  • 5
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng Q., Li H., Merdek K., Park J.T. Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. Journal of Bacteriology 2000, 182:4836-4840.
    • (2000) Journal of Bacteriology , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 6
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland W.W. Statistical analysis of enzyme kinetic data. Methods in Enzymology 1979, 63:103-138.
    • (1979) Methods in Enzymology , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 8
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-d-glucosaminidase from rat spleen cytosol
    • Dong D.L.Y., Hart G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-d-glucosaminidase from rat spleen cytosol. Journal of Biological Chemistry 1994, 269:19321-19330.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 19321-19330
    • Dong, D.L.Y.1    Hart, G.W.2
  • 9
    • 0027328373 scopus 로고
    • Glycosylation of mammalian neurofilaments-localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides-L and polypeptides-M
    • Dong D.L.Y., Xu Z.S., Chevrier M.R., Cotter R.J., Cleveland D.W., Hart G.W. Glycosylation of mammalian neurofilaments-localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides-L and polypeptides-M. Journal of Biological Chemistry 1993, 268:16679-16687.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 16679-16687
    • Dong, D.L.Y.1    Xu, Z.S.2    Chevrier, M.R.3    Cotter, R.J.4    Cleveland, D.W.5    Hart, G.W.6
  • 11
    • 0015244836 scopus 로고
    • Reporter group at the active site of acetoacetate decarboxylase. I. Ionization constant of the nitrophenol
    • Frey P.A., Kokesh F.C., Westheimer F.H. Reporter group at the active site of acetoacetate decarboxylase. I. Ionization constant of the nitrophenol. Journal of the American Chemical Society 1971, 93:7266-7269.
    • (1971) Journal of the American Chemical Society , vol.93 , pp. 7266-7269
    • Frey, P.A.1    Kokesh, F.C.2    Westheimer, F.H.3
  • 14
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R., Brunak S. Prediction of glycosylation across the human proteome and the correlation to protein function. Pacific Symposium on Biocomputing 2002, 310-322.
    • (2002) Pacific Symposium on Biocomputing , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 15
    • 84867167595 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc-modified proteins in published large-scale proteome data
    • Hahne H., Gholami A.M., Kuster B. Discovery of O-GlcNAc-modified proteins in published large-scale proteome data. Molecular & Cellular Proteomics 2012, 11:843-850.
    • (2012) Molecular & Cellular Proteomics , vol.11 , pp. 843-850
    • Hahne, H.1    Gholami, A.M.2    Kuster, B.3
  • 17
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate
    • Haltiwanger R.S., Grove K., Philipsberg G.A. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate. Journal of Biological Chemistry 1998, 273:3611-3617.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 18
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins-identification of a uridine diphospho-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger R.S., Holt G.D., Hart G.W. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins-identification of a uridine diphospho-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase. Journal of Biological Chemistry 1990, 265:2563-2568.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 20
    • 65349126348 scopus 로고    scopus 로고
    • Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle
    • Hedou J., Bastide B., Page A., Michalski J.C., Morelle W. Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle. Proteomics 2009, 9:2139-2148.
    • (2009) Proteomics , vol.9 , pp. 2139-2148
    • Hedou, J.1    Bastide, B.2    Page, A.3    Michalski, J.C.4    Morelle, W.5
  • 21
    • 0025782244 scopus 로고
    • N-Acetylglucosamino-1,5-lactone oxime and the corresponding (phenylcarbamoyl)oxime-novel and potent inhibitors of beta-N-acetylglucosaminidase
    • Horsch M., Hoesch L., Vasella A., Rast D.M. N-Acetylglucosamino-1,5-lactone oxime and the corresponding (phenylcarbamoyl)oxime-novel and potent inhibitors of beta-N-acetylglucosaminidase. European Journal of Biochemistry 1991, 197:815-818.
    • (1991) European Journal of Biochemistry , vol.197 , pp. 815-818
    • Horsch, M.1    Hoesch, L.2    Vasella, A.3    Rast, D.M.4
  • 24
    • 0037533891 scopus 로고    scopus 로고
    • Dynamic glycosylation of the transcription factor CREB: a potential role in gene regulation
    • Lamarre-Vincent N., Hsieh-Wilson L.C. Dynamic glycosylation of the transcription factor CREB: a potential role in gene regulation. Journal of the American Chemical Society 2003, 125:6612-6613.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 6612-6613
    • Lamarre-Vincent, N.1    Hsieh-Wilson, L.C.2
  • 25
    • 33646159532 scopus 로고    scopus 로고
    • Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates
    • Lazarus B.D., Love D.C., Hanover J.A. Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates. Glycobiology 2006, 16:415-421.
    • (2006) Glycobiology , vol.16 , pp. 415-421
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 28
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 2011, 469:564-567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 29
    • 34250309514 scopus 로고    scopus 로고
    • A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates
    • Leavy T.M., Bertozzi C.R. A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates. Bioorganic & Medicinal Chemistry Letters 2007, 17:3851-3854.
    • (2007) Bioorganic & Medicinal Chemistry Letters , vol.17 , pp. 3851-3854
    • Leavy, T.M.1    Bertozzi, C.R.2
  • 30
    • 33746904776 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1
    • Lim K.H., Chang H.I. O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1. FEBS Letters 2006, 580:4645-4652.
    • (2006) FEBS Letters , vol.580 , pp. 4645-4652
    • Lim, K.H.1    Chang, H.I.2
  • 31
    • 0036091929 scopus 로고    scopus 로고
    • Production of O-GlcNAc modified recombinant proteins in Escherichia coli
    • Lim K.H., Ha C.H., Chang H.I. Production of O-GlcNAc modified recombinant proteins in Escherichia coli. Journal of Microbiology and Biotechnology 2002, 12:306-311.
    • (2002) Journal of Microbiology and Biotechnology , vol.12 , pp. 306-311
    • Lim, K.H.1    Ha, C.H.2    Chang, H.I.3
  • 33
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase-domain structure and substrate specificity
    • Lubas W.A., Hanover J.A. Functional expression of O-linked GlcNAc transferase-domain structure and substrate specificity. Journal of Biological Chemistry 2000, 275:10983-10988.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 34
    • 0020560713 scopus 로고
    • Pool levels of UDP-N-acetylglucosamine and UDP-N-acetylglucosamine-enolpyruvate in Escherichia-coli and correlation with peptidoglycan synthesis
    • Menginlecreulx D., Flouret B., Vanheijenoort J. Pool levels of UDP-N-acetylglucosamine and UDP-N-acetylglucosamine-enolpyruvate in Escherichia-coli and correlation with peptidoglycan synthesis. Journal of Bacteriology 1983, 154:1284-1290.
    • (1983) Journal of Bacteriology , vol.154 , pp. 1284-1290
    • Menginlecreulx, D.1    Flouret, B.2    Vanheijenoort, J.3
  • 35
    • 0021232930 scopus 로고
    • Reciprocal intrapool variation in plasmid copy numbers-a characteristic of segregational incompatibility
    • Projan S.J., Novick R.P. Reciprocal intrapool variation in plasmid copy numbers-a characteristic of segregational incompatibility. Plasmid 1984, 12:52-60.
    • (1984) Plasmid , vol.12 , pp. 52-60
    • Projan, S.J.1    Novick, R.P.2
  • 36
    • 44649107616 scopus 로고    scopus 로고
    • Sp1 modulates ncOGT activity to alter target recognition and enhanced thermotolerance in E-coli
    • Riu I.H., Shin I.S., Do S.I. Sp1 modulates ncOGT activity to alter target recognition and enhanced thermotolerance in E-coli. Biochemical and Biophysical Research Communications 2008, 372:203-209.
    • (2008) Biochemical and Biophysical Research Communications , vol.372 , pp. 203-209
    • Riu, I.H.1    Shin, I.S.2    Do, S.I.3
  • 38
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: implications for cancer cell biology
    • Slawson C., Hart G.W. O-GlcNAc signalling: implications for cancer cell biology. Nature Reviews Cancer 2011, 11:678-684.
    • (2011) Nature Reviews Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 39
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance
    • Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance. Journal of Biological Chemistry 2007, 282:21382-21391.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 40
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a beta-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta-lactamase induction
    • Votsch W., Templin M.F. Characterization of a beta-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta-lactamase induction. Journal of Biological Chemistry 2000, 275:39032-39038.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 39032-39038
    • Votsch, W.1    Templin, M.F.2
  • 41
    • 79953652899 scopus 로고    scopus 로고
    • DbOGAP-an integrated bioinformatics resource for protein O-GlcNAcylation
    • Wang J., Torii M., Liu H., Hart G., Hu Z.-Z. dbOGAP-an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinformatics 2011, 12:91.
    • (2011) BMC Bioinformatics , vol.12 , pp. 91
    • Wang, J.1    Torii, M.2    Liu, H.3    Hart, G.4    Hu, Z.-Z.5
  • 42
    • 77952555814 scopus 로고    scopus 로고
    • Structural genomics-impact on biomedicine and drug discovery
    • Weigelt J. Structural genomics-impact on biomedicine and drug discovery. Experimental Cell Research 2010, 316:1332-1338.
    • (2010) Experimental Cell Research , vol.316 , pp. 1332-1338
    • Weigelt, J.1
  • 43
    • 0017288319 scopus 로고
    • Isolation of Escherichia-coli K-12 mutants with altered levels of beta-N-acetylglucosaminidase
    • Yem D.W., Wu H.C. Isolation of Escherichia-coli K-12 mutants with altered levels of beta-N-acetylglucosaminidase. Journal of Bacteriology 1976, 125:372-373.
    • (1976) Journal of Bacteriology , vol.125 , pp. 372-373
    • Yem, D.W.1    Wu, H.C.2
  • 44
    • 0017228929 scopus 로고
    • Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli
    • Yem D.W., Wu H.C. Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli. Journal of Bacteriology 1976, 125:324-331.
    • (1976) Journal of Bacteriology , vol.125 , pp. 324-331
    • Yem, D.W.1    Wu, H.C.2
  • 45


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