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Volumn 278, Issue 7, 2011, Pages 1086-1097

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

Author keywords

2 oxoglutarate dependent dioxygenase; ankyrin repeat domain; factor inhibiting HIF; histidinyl hydroxylation; post translational hydroxylation

Indexed keywords

2 OXOGLUTARIC ACID; ANKYRIN; HISTIDINE; HYPOXIA INDUCIBLE FACTOR; PEPTIDE FRAGMENT; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; SYNTHETIC PEPTIDE; TANKYRASE; TANKYRASE 2; UNCLASSIFIED DRUG;

EID: 79952858715     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08022.x     Document Type: Article
Times cited : (69)

References (36)
  • 1
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • DOI 10.1101/gad.991402
    • Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, &, Bruick RK, (2002) FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 16, 1466-1471. (Pubitemid 34686328)
    • (2002) Genes and Development , vol.16 , Issue.12 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 3
    • 77956631879 scopus 로고    scopus 로고
    • Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen
    • Flashman E, Hoffart LM, Hamed RB, Bollinger JM Jr, Krebs C, &, Schofield CJ, (2010) Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen. FEBS J 277, 4089-4099.
    • (2010) FEBS J , vol.277 , pp. 4089-4099
    • Flashman, E.1    Hoffart, L.M.2    Hamed, R.B.3    Bollinger, Jr.J.M.4    Krebs, C.5    Schofield, C.J.6
  • 4
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic Properties of the Asparaginyl Hydroxylase (FIH) in the Oxygen Sensing Pathway Are Distinct from Those of Its Prolyl 4-Hydroxylases
    • DOI 10.1074/jbc.M312254200
    • Koivunen P, Hirsila M, Gunzler V, Kivirikko KI, &, Myllyharju J, (2004) Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. J Biol Chem 279, 9899-9904. (Pubitemid 38372589)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 7
    • 34548794831 scopus 로고    scopus 로고
    • ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism
    • DOI 10.1128/MCB.00511-07
    • Ferguson JE III, Wu Y, Smith K, Charles P, Powers K, Wang H, &, Patterson C, (2007) ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Mol Cell Biol 27, 6407-6419. (Pubitemid 47435747)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.18 , pp. 6407-6419
    • Ferguson III, J.E.1    Wu, Y.2    Smith, K.3    Charles, P.4    Powers, K.5    Wang, H.6    Patterson, C.7
  • 8
    • 63049120802 scopus 로고    scopus 로고
    • Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins
    • Cockman ME, Webb JD, Kramer HB, Kessler BM, &, Ratcliffe PJ, (2009) Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins. Mol Cell Proteomics 8, 535-546.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 535-546
    • Cockman, M.E.1    Webb, J.D.2    Kramer, H.B.3    Kessler, B.M.4    Ratcliffe, P.J.5
  • 9
    • 66549122493 scopus 로고    scopus 로고
    • MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)
    • Webb JD, Muranyi A, Pugh CW, Ratcliffe PJ, &, Coleman ML, (2009) MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). Biochem J 420, 327-333.
    • (2009) Biochem J , vol.420 , pp. 327-333
    • Webb, J.D.1    Muranyi, A.2    Pugh, C.W.3    Ratcliffe, P.J.4    Coleman, M.L.5
  • 11
    • 69749089963 scopus 로고    scopus 로고
    • Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function
    • Hardy AP, Prokes I, Kelly L, Campbell ID, &, Schofield CJ, (2009) Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function. J Mol Biol 392, 994-1006.
    • (2009) J Mol Biol , vol.392 , pp. 994-1006
    • Hardy, A.P.1    Prokes, I.2    Kelly, L.3    Campbell, I.D.4    Schofield, C.J.5
  • 12
    • 70350389957 scopus 로고    scopus 로고
    • FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins
    • Cockman ME, Webb JD, &, Ratcliffe PJ, (2009) FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins. Ann NY Acad Sci 1177, 9-18.
    • (2009) Ann NY Acad Sci , vol.1177 , pp. 9-18
    • Cockman, M.E.1    Webb, J.D.2    Ratcliffe, P.J.3
  • 13
    • 77957912885 scopus 로고    scopus 로고
    • Hypoxia-dependent sequestration of an oxygen sensor by a widespread structural motif can shape the hypoxic response - A predictive kinetic model
    • 139.
    • Schmierer B, Novak B, &, Schofield CJ, (2010) Hypoxia-dependent sequestration of an oxygen sensor by a widespread structural motif can shape the hypoxic response-a predictive kinetic model. BMC Syst Biol 4, 139.
    • (2010) BMC Syst Biol , vol.4
    • Schmierer, B.1    Novak, B.2    Schofield, C.J.3
  • 15
    • 36749045682 scopus 로고    scopus 로고
    • Tankyrase function at telomeres, spindle poles, and beyond
    • DOI 10.1016/j.biochi.2007.07.012, PII S0300908407001885, Telomeres and Telomerase: from Basic Research to Clinical Applications
    • Hsiao SJ, &, Smith S, (2008) Tankyrase function at telomeres, spindle poles, and beyond. Biochimie 90, 83-92. (Pubitemid 350216209)
    • (2008) Biochimie , vol.90 , Issue.1 , pp. 83-92
    • Hsiao, S.J.1    Smith, S.2
  • 16
    • 0036846033 scopus 로고    scopus 로고
    • Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803
    • DOI 10.1042/BJ20021162
    • McNeill LA, Hewitson KS, Claridge TD, Seibel JF, Horsfall LE, &, Schofield CJ, (2002) Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. Biochem J 367, 571-575. (Pubitemid 35305697)
    • (2002) Biochemical Journal , vol.367 , Issue.3 , pp. 571-575
    • McNeill, L.A.1    Hewitson, K.S.2    Claridge, T.D.3    Seibel, J.F.4    Horsfall, L.E.5    Schofield, C.J.6
  • 18
    • 54749094325 scopus 로고    scopus 로고
    • Auto-hydroxylation of FIH-1: An Fe(II), alpha-ketoglutarate-dependent human hypoxia sensor
    • Chen YH, Comeaux LM, Eyles SJ, &, Knapp MJ, (2008) Auto-hydroxylation of FIH-1: an Fe(II), alpha-ketoglutarate-dependent human hypoxia sensor. Chem Commun (Camb) 39, 4768-4770.
    • (2008) Chem Commun (Camb) , vol.39 , pp. 4768-4770
    • Chen, Y.H.1    Comeaux, L.M.2    Eyles, S.J.3    Knapp, M.J.4
  • 21
    • 33846400822 scopus 로고    scopus 로고
    • The most versatile of all reactive intermediates?
    • DOI 10.1038/nchembio0207-86, PII NCHEMBIO020786
    • Flashman E, &, Schofield CJ, (2007) The most versatile of all reactive intermediates? Nat Chem Biol 3, 86-87. (Pubitemid 46134991)
    • (2007) Nature Chemical Biology , vol.3 , Issue.2 , pp. 86-87
    • Flashman, E.1    Schofield, C.J.2
  • 23
    • 77954219049 scopus 로고    scopus 로고
    • Multifunctional flavonoid dioxygenases: Flavonol and anthocyanin biosynthesis in Arabidopsis thaliana L
    • Martens S, Preuss A, &, Matern U, (2010) Multifunctional flavonoid dioxygenases: flavonol and anthocyanin biosynthesis in Arabidopsis thaliana L. Phytochemistry 71, 1040-1049.
    • (2010) Phytochemistry , vol.71 , pp. 1040-1049
    • Martens, S.1    Preuss, A.2    Matern, U.3
  • 24
    • 63049095888 scopus 로고    scopus 로고
    • Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1)
    • Wilkins SE, Hyvarinen J, Chicher J, Gorman JJ, Peet DJ, Bilton RL, &, Koivunen P, (2009) Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1). Int J Biochem Cell Biol 41, 1563-1571.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1563-1571
    • Wilkins, S.E.1    Hyvarinen, J.2    Chicher, J.3    Gorman, J.J.4    Peet, D.J.5    Bilton, R.L.6    Koivunen, P.7
  • 26
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440, 363-367.
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 27
    • 0033835373 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase
    • Du L, Sanchez C, Chen M, Edwards DJ, &, Shen B, (2000) The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase. Chem Biol 7, 623-642.
    • (2000) Chem Biol , vol.7 , pp. 623-642
    • Du, L.1    Sanchez, C.2    Chen, M.3    Edwards, D.J.4    Shen, B.5
  • 28
    • 0028555351 scopus 로고
    • Gene organization in the bleomycin-resistance region of the producer organism Streptomyces verticillus
    • Calcutt MJ, &, Schmidt FJ, (1994) Gene organization in the bleomycin-resistance region of the producer organism Streptomyces verticillus. Gene 151, 17-21.
    • (1994) Gene , vol.151 , pp. 17-21
    • Calcutt, M.J.1    Schmidt, F.J.2
  • 29
    • 0036008124 scopus 로고    scopus 로고
    • Formation of β-hydroxy histidine in the biosynthesis of nikkomycin antibiotics
    • DOI 10.1016/S1074-5521(02)00090-X, PII S107455210200090X
    • Chen H, Hubbard BK, O'Connor SE, &, Walsh CT, (2002) Formation of beta-hydroxy histidine in the biosynthesis of nikkomycin antibiotics. Chem Biol 9, 103-112. (Pubitemid 34155869)
    • (2002) Chemistry and Biology , vol.9 , Issue.1 , pp. 103-112
    • Chen, H.1    Hubbard, B.K.2    O'Connor, S.E.3    Walsh, C.T.4
  • 30
    • 5644240828 scopus 로고    scopus 로고
    • Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (HIF) in regulating HIF transcriptional target genes
    • DOI 10.1074/jbc.M406713200
    • Stolze IP, Tian YM, Appelhoff RJ, Turley H, Wykoff CC, Gleadle JM, &, Ratcliffe PJ, (2004) Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (HIF) in regulating HIF transcriptional target genes. J Biol Chem 279, 42719-42725. (Pubitemid 39372158)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 42719-42725
    • Stolze, I.P.1    Tian, Y.-M.2    Appelhoff, R.J.3    Turley, H.4    Wykoff, C.C.5    Gleadle, J.M.6    Ratcliffe, P.J.7
  • 31
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter G, (2010) xia2: an expert system for macromolecular crystallography data reduction. J Appl Crystallogr 43, 186-190.
    • (2010) J Appl Crystallogr , vol.43 , pp. 186-190
    • Winter, G.1
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Bailey S, (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50, 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, &, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26, 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 0036472339 scopus 로고    scopus 로고
    • Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)
    • DOI 10.1042/0264-6021:3610451
    • Sbodio JI, Lodish HF, &, Chi NW, (2002) Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase). Biochem J 361, 451-459. (Pubitemid 34177814)
    • (2002) Biochemical Journal , vol.361 , Issue.3 , pp. 451-459
    • Sbodio, J.I.1    Lodish, H.F.2    Chi, N.-W.3


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