메뉴 건너뛰기




Volumn 16, Issue 1, 1999, Pages 91-106

Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50→Arg

Author keywords

Amino acids; eIF 5A; Hypusine; Post translational modification; Protein folding

Indexed keywords

CYSTEINE; GUANIDINE; INITIATION FACTOR 5A; PROTEIN PRECURSOR; TYROSINE;

EID: 0032976399     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01318888     Document Type: Article
Times cited : (3)

References (42)
  • 1
    • 0023871286 scopus 로고
    • Developmental pattern for deoxyhypusine hydroxylase in rat brain
    • Abbruzzese A (1988) Developmental pattern for deoxyhypusine hydroxylase in rat brain. J Neurochem 50: 695-699
    • (1988) J Neurochem , vol.50 , pp. 695-699
    • Abbruzzese, A.1
  • 2
    • 0021948742 scopus 로고
    • Deoxyhypusine hydroxylase: Distribution and partial purification from rat testis
    • Abbruzzese A, Park MH, Folk JE (1985) Deoxyhypusine hydroxylase: distribution and partial purification from rat testis. Fed Proc 44: 1487
    • (1985) Fed Proc , vol.44 , pp. 1487
    • Abbruzzese, A.1    Park, M.H.2    Folk, J.E.3
  • 3
    • 0022973967 scopus 로고
    • Deoxhypusine hydroxylase from rat testis. Partial purification and characterization
    • Abbruzzese A, Park MH, Folk JE (1986) Deoxhypusine hydroxylase from rat testis. Partial purification and characterization. J Biol Chem 261: 3085-3089
    • (1986) J Biol Chem , vol.261 , pp. 3085-3089
    • Abbruzzese, A.1    Park, M.H.2    Folk, J.E.3
  • 4
    • 0002123870 scopus 로고
    • Polyamine-dependent post-translational modification of protein and cell proliferation
    • Perin A et al (eds) Wichtig ED, Milan
    • Abbruzzese A, Isernia T, Liguori V, Beninati S (1988a) Polyamine-dependent post-translational modification of protein and cell proliferation. In: Perin A et al (eds) Perspective in polyamine research. Wichtig ED, Milan, pp 79-84
    • (1988) Perspective in Polyamine Research , pp. 79-84
    • Abbruzzese, A.1    Isernia, T.2    Liguori, V.3    Beninati, S.4
  • 6
    • 0024462317 scopus 로고
    • Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide
    • Abbruzzese A, Park MH, Beninati S, Folk JE (1989) Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide. Biochem Biophys Acta 997: 248-255
    • (1989) Biochem Biophys Acta , vol.997 , pp. 248-255
    • Abbruzzese, A.1    Park, M.H.2    Beninati, S.3    Folk, J.E.4
  • 7
    • 0026027968 scopus 로고
    • The active site of deoxyhypusyl hydroxylase: Use of catecholpeptides and their component chelator and peptide moieties as molecular probes
    • Abbruzzese A, Hanauske-Abel HM, Park MH, Henke S, Folk JE (1991) The active site of deoxyhypusyl hydroxylase: use of catecholpeptides and their component chelator and peptide moieties as molecular probes. Biochem Biophys Acta 1077: 159-166
    • (1991) Biochem Biophys Acta , vol.1077 , pp. 159-166
    • Abbruzzese, A.1    Hanauske-Abel, H.M.2    Park, M.H.3    Henke, S.4    Folk, J.E.5
  • 8
    • 0024412497 scopus 로고
    • Mutational effects on protein stability
    • Alber TJ (1989) Mutational effects on protein stability. Annu Rev Biochem 58: 765-798
    • (1989) Annu Rev Biochem , vol.58 , pp. 765-798
    • Alber, T.J.1
  • 9
    • 0020505379 scopus 로고
    • Structural homology of lens crystallins. A method to detect protein structural homology from primary sequences
    • Argos P, Siezen BJ (1983) Structural homology of lens crystallins. A method to detect protein structural homology from primary sequences. Eur J Biochem 131: 143-148
    • (1983) Eur J Biochem , vol.131 , pp. 143-148
    • Argos, P.1    Siezen, B.J.2
  • 10
    • 0025141231 scopus 로고
    • High-performance liquid chromatographie method for determination of hypusine and deoxyhypusine
    • Beninati S, Abbruzzese A, Folk JE (1990) High-performance liquid Chromatographie method for determination of hypusine and deoxyhypusine. Anal Biochem 184: 16-20
    • (1990) Anal Biochem , vol.184 , pp. 16-20
    • Beninati, S.1    Abbruzzese, A.2    Folk, J.E.3
  • 11
    • 0028955591 scopus 로고
    • Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A
    • Beninati S, Nicolini L, Jakus J, Passeggio, Abbruzzese A (1995) Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A. Biochem J 305: 725-728
    • (1995) Biochem J , vol.305 , pp. 725-728
    • Beninati, S.1    Nicolini, L.2    Jakus, J.3    Passeggio4    Abbruzzese, A.5
  • 13
    • 0025856806 scopus 로고
    • Denaturated states of proteins
    • Dill KA, Shortle D (1991) Denaturated states of proteins. Annu Rev Biochem 60: 795-825
    • (1991) Annu Rev Biochem , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 15
    • 0015871219 scopus 로고
    • Spectrophotometric titration of the functional groups of proteins
    • Donovan JW (1973) Spectrophotometric titration of the functional groups of proteins. Methods Enzymol 27: 525-548
    • (1973) Methods Enzymol , vol.27 , pp. 525-548
    • Donovan, J.W.1
  • 16
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins
    • Eftink MR, Ghiron CA (1976) Exposure of tryptophanyl residues in proteins. Biochemistry 15: 672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 17
    • 0023830955 scopus 로고
    • Structure and stability of thermophilic enzymes. Studies on thermolysin
    • Fontana A (1988) Structure and stability of thermophilic enzymes. Studies on thermolysin. Biophys Chem 29: 181-193
    • (1988) Biophys Chem , vol.29 , pp. 181-193
    • Fontana, A.1
  • 18
    • 0024296987 scopus 로고
    • Oligonucleotide-directed constructions of mutations: A gapped duplex DNA procedure without enzymatic reactions in vitro
    • Fritz HJ, Hohlmaier J, Kramer W, Ohmayer A, Wippler J (1988) Oligonucleotide-directed constructions of mutations: a gapped duplex DNA procedure without enzymatic reactions in vitro. Nucleic Acid Res 16: 6987-6999
    • (1988) Nucleic Acid Res , vol.16 , pp. 6987-6999
    • Fritz, H.J.1    Hohlmaier, J.2    Kramer, W.3    Ohmayer, A.4    Wippler, J.5
  • 19
    • 0023471291 scopus 로고
    • Eukaryotic initiation factor 4D, the hypusine containing protein, is conserved among eukaryotes
    • Gordon ED, Mora R, Meredith SC, Lee C, Lindquist SL (1987) Eukaryotic initiation factor 4D, the hypusine containing protein, is conserved among eukaryotes. J Biol Chem 262: 16585-16589
    • (1987) J Biol Chem , vol.262 , pp. 16585-16589
    • Gordon, E.D.1    Mora, R.2    Meredith, S.C.3    Lee, C.4    Lindquist, S.L.5
  • 20
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey JWB (1991) Translational control in mammalian cells. Annu Rev Biochem 60: 717-755
    • (1991) Annu Rev Biochem , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 21
    • 0025087875 scopus 로고
    • The role of mammalian initiation factor eIF-4D and its hypusine modification in translation
    • Hershey JWB, Smit-McBride Z, Schnier J (1990) The role of mammalian initiation factor eIF-4D and its hypusine modification in translation. Biochim Biophys Acta 1050: 160-162
    • (1990) Biochim Biophys Acta , vol.1050 , pp. 160-162
    • Hershey, J.W.B.1    Smit-McBride, Z.2    Schnier, J.3
  • 22
    • 0027518126 scopus 로고
    • Features of the spermidine-binding site of deoxyhypusine synthase as derived from inhibition studies
    • Jakus J, Wolff EC, Park MH, Folk JE (1993) Features of the spermidine-binding site of deoxyhypusine synthase as derived from inhibition studies. J Biol Chem 268: 13151-13159
    • (1993) J Biol Chem , vol.268 , pp. 13151-13159
    • Jakus, J.1    Wolff, E.C.2    Park, M.H.3    Folk, J.E.4
  • 23
    • 0028829801 scopus 로고
    • The polypeptide chain of eukaryotic initiation factor 5A occurs in two distinct conformations in the absence of the hypusine modification
    • Joao HC, Csonga R, Klier H, Koettnitz K, Auer M, Eder J (1995) The polypeptide chain of eukaryotic initiation factor 5A occurs in two distinct conformations in the absence of the hypusine modification. Biochemistry 34: 14703-14711
    • (1995) Biochemistry , vol.34 , pp. 14703-14711
    • Joao, H.C.1    Csonga, R.2    Klier, H.3    Koettnitz, K.4    Auer, M.5    Eder, J.6
  • 24
    • 0018726846 scopus 로고
    • A fluorescence derivative of ribosomal protein S18 which permits direct observation of messenger RNA binding
    • Kang C, Wells B, Cantor CR (1979) A fluorescence derivative of ribosomal protein S18 which permits direct observation of messenger RNA binding. J Biol Chem 254: 6667-6672
    • (1979) J Biol Chem , vol.254 , pp. 6667-6672
    • Kang, C.1    Wells, B.2    Cantor, C.R.3
  • 25
    • 0028852113 scopus 로고
    • Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF5A from HeLa cells
    • Klier H, Csonga R, Joao HC, Eckerskorn C, Auer M, Lottspeich F, Eder J (1995) Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF5A from HeLa cells. Biochemistry 34: 14693-14702
    • (1995) Biochemistry , vol.34 , pp. 14693-14702
    • Klier, H.1    Csonga, R.2    Joao, H.C.3    Eckerskorn, C.4    Auer, M.5    Lottspeich, F.6    Eder, J.7
  • 27
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model-compounds and of lysozyme by iodide ion
    • Lehrer SS (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model-compounds and of lysozyme by iodide ion. Biochemistry 10: 3254
    • (1971) Biochemistry , vol.10 , pp. 3254
    • Lehrer, S.S.1
  • 31
    • 0021759446 scopus 로고
    • The mammalian hypusine-containing protein, eukaryotic initiation factor 4D
    • Park MH, Chung SI, Cooper HL, Folk JE (1984) The mammalian hypusine-containing protein, eukaryotic initiation factor 4D. J Biol Chem 259: 4563-4565
    • (1984) J Biol Chem , vol.259 , pp. 4563-4565
    • Park, M.H.1    Chung, S.I.2    Cooper, H.L.3    Folk, J.E.4
  • 32
    • 0025824235 scopus 로고
    • Comparison of the activities of variant forms of eIF-4D: The requirement for hypusine or deoxyhypusine
    • Park MH, Wolff EC, Smith-McBride Z, Hershey JWB, Folk JE (1991) Comparison of the activities of variant forms of eIF-4D: the requirement for hypusine or deoxyhypusine. J Biol Chem 266: 7988-7994
    • (1991) J Biol Chem , vol.266 , pp. 7988-7994
    • Park, M.H.1    Wolff, E.C.2    Smith-McBride, Z.3    Hershey, J.W.B.4    Folk, J.E.5
  • 33
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • Park MH, Wolff EC, Folk JE (1993) Is hypusine essential for eukaryotic cell proliferation? Trends Biochem Sci 18: 475-479
    • (1993) Trends Biochem Sci , vol.18 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 34
    • 0027944561 scopus 로고
    • Antiproliferative effects of inhibitors of deoxyhypusine synthase
    • Park MH, Wolff EC, Lee YB, Folk JE (1994) Antiproliferative effects of inhibitors of deoxyhypusine synthase. J Biol Chem 269: 27827-27832
    • (1994) J Biol Chem , vol.269 , pp. 27827-27832
    • Park, M.H.1    Wolff, E.C.2    Lee, Y.B.3    Folk, J.E.4
  • 35
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second-derivative spectroscopy
    • Ragone R, Colonna G, Balestrieri C, Servillo L, Irace G (1984) Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 23: 1871-1875
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 36
    • 0023219317 scopus 로고
    • Unfolding pathway of myoglobin: Effect of denaturants in solvent accessibility to tyrosyl residues detected by second-derivative spectroscopy
    • Ragone R, Colonna G, Bismuto E, Irace G (1987) Unfolding pathway of myoglobin: effect of denaturants in solvent accessibility to tyrosyl residues detected by second-derivative spectroscopy. Biochemistry 26: 2130-2134
    • (1987) Biochemistry , vol.26 , pp. 2130-2134
    • Ragone, R.1    Colonna, G.2    Bismuto, E.3    Irace, G.4
  • 38
    • 0025810272 scopus 로고
    • Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae
    • Schnier J, Schwelbeerger HG, Smit-McBride Z, Kang HA, Hershey JWB (1991) Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 11: 3105-3114
    • (1991) Mol Cell Biol , vol.11 , pp. 3105-3114
    • Schnier, J.1    Schwelbeerger, H.G.2    Smit-McBride, Z.3    Kang, H.A.4    Hershey, J.W.B.5
  • 40
    • 0027050824 scopus 로고
    • Modeling the effects of mutations on the denaturated states of protein
    • Shortle D, Chan HS, Dill KA (1992) Modeling the effects of mutations on the denaturated states of protein. Protein Sci 1: 210-215
    • (1992) Protein Sci , vol.1 , pp. 210-215
    • Shortle, D.1    Chan, H.S.2    Dill, K.A.3
  • 41
    • 0024509495 scopus 로고
    • Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein
    • Smit-McBride Z, Dever TE, Hershey JWB, Merrick WC (1989) Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein. J Biol Chem 264: 1578-1583
    • (1989) J Biol Chem , vol.264 , pp. 1578-1583
    • Smit-McBride, Z.1    Dever, T.E.2    Hershey, J.W.B.3    Merrick, W.C.4
  • 42
    • 0001253507 scopus 로고
    • Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes
    • Willis KJ, Szabo AG (1991) Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes. J Phys Chem 95: 1585-1589
    • (1991) J Phys Chem , vol.95 , pp. 1585-1589
    • Willis, K.J.1    Szabo, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.