메뉴 건너뛰기




Volumn 16, Issue 10, 2010, Pages 1968-1979

Probing tRNA interaction with biogenic polyamines

Author keywords

Affinity capillary electrophoresis (ACE); Binding constant; Condensation; FTIR spectroscopy; Hyperchromism; Hypochromism; Polyamines; Preferential binding site; tRNA; tRNA stability

Indexed keywords

COBALT HEXAMINE; MESSENGER RNA; METHENAMINE; PUTRESCINE; RIBOSOME RNA; SPERMIDINE; SPERMINE; TRANSFER RNA; UNCLASSIFIED DRUG; COBALT; COBALT AMMONIUM COMPLEX; FUNGAL RNA; POLYAMINE;

EID: 77957303874     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1994310     Document Type: Article
Times cited : (63)

References (60)
  • 1
    • 0033605751 scopus 로고    scopus 로고
    • Effect of buffer conditions on the position of tRNA on the 70 S ribosome as visualized by cryoelectron microscopy
    • DOI 10.1074/jbc.274.13.8723
    • Agrawal RK, Penczek P, Grassucci RA, Burkhardt N, Nierhaus KH, Frank J. 1999. Effect of buffer conditions on the position of tRNA on the 70 S ribosome as visualized by cryoelectron microscopy. J Biol Chem 274: 8723-8729. (Pubitemid 29164669)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8723-8729
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Burkhardt, N.4    Nierhaus, K.H.5    Frankt, J.6
  • 2
    • 4744371427 scopus 로고    scopus 로고
    • Structural analysis of DNA interactions with biogenic polyamines and cobalt(III)hexamine studied by Fourier transform infrared and capillary electrophoresis
    • Ahmed Ouameur A, Tajmir-Riahi HA. 2004. Structural analysis of DNA interactions with biogenic polyamines and cobalt(III)hexamine studied by Fourier transform infrared and capillary electrophoresis. J Biol Chem 279: 42041-42054.
    • (2004) J Biol Chem , vol.279 , pp. 42041-42054
    • Ahmed Ouameur, A.1    Tajmir-Riahi, H.A.2
  • 5
    • 0034307464 scopus 로고    scopus 로고
    • Photoaffinity polyamines: Interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes
    • Amarantos I, Kalpaxis DL. 2000. Photoaffinity polyamines: Interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes. Nucleic Acids Res 28: 3733-3742.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3733-3742
    • Amarantos, I.1    Kalpaxis, D.L.2
  • 6
    • 0034616327 scopus 로고    scopus 로고
    • A comparative study of calf-thymus DNA binding to Cr(III) and Cr(VI) ions: Evidence for the guanine N-7 chromium-phosphate chelate formation
    • Arakawa H, Ahmad R, Naoui M, Tajmir-Riahi HA. 2000. A comparative study of calf-thymus DNA binding to Cr(III) and Cr(VI) ions: Evidence for the guanine N-7 chromium-phosphate chelate formation. J Biol Chem 275: 10150-10153.
    • (2000) J Biol Chem , vol.275 , pp. 10150-10153
    • Arakawa, H.1    Ahmad, R.2    Naoui, M.3    Tajmir-Riahi, H.A.4
  • 7
    • 0034874536 scopus 로고    scopus 로고
    • Silver(I) complexes with DNA and RNA studied by Fourier transform infrared spectroscopy and capillary electrophoresis
    • Arakawa H, Neault J-F, Tajmir-Riahi HA. 2001. Silver(I) complexes with DNA and RNA studied by Fourier transform infrared spectroscopy and capillary electrophoresis. Biophys J 81: 1580-1587.
    • (2001) Biophys J , vol.81 , pp. 1580-1587
    • Arakawa, H.1    Neault, J.-F.2    Tajmir-Riahi, H.A.3
  • 9
    • 28444461786 scopus 로고    scopus 로고
    • Naturally occurring polyamines: Interaction with macromolecules
    • Bachrach U. 2005. Naturally occurring polyamines: Interaction with macromolecules. Curr Protein Pept Sci 6: 559-566.
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 559-566
    • Bachrach, U.1
  • 10
    • 0033214629 scopus 로고    scopus 로고
    • The non-enzymatic hydrolysis of oligoribonucleotides. VI. The role of biogenic polyamines
    • Bibillo A, Figlerowicz M, Kierzek R. 1999. The non-enzymatic hydrolysis of oligoribonucleotides. VI. The role of biogenic polyamines. Nucleic Acids Res 27: 3931-3937.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3931-3937
    • Bibillo, A.1    Figlerowicz, M.2    Kierzek, R.3
  • 11
    • 0017802657 scopus 로고
    • Hydrogen bonding interactions of polyamines with the 2′OH of RNA
    • Bolton PH, Kearns DR. 1978. Hydrogen bonding interactions of polyamines with the 2′OH of RNA. Nucleic Acids Res 5: 1315-1324.
    • (1978) Nucleic Acids Res , vol.5 , pp. 1315-1324
    • Bolton, P.H.1    Kearns, D.R.2
  • 12
    • 0014725117 scopus 로고
    • Oligonucleotide interactions. III. Circular dichroism studies of the conformation of deoxyoligonucleotides
    • Cantor CR, Warshaw MM, Shapiro H. 1970. Oligonucleotide interactions. III. Circular dichroism studies of the conformation of deoxyoligonucleotides. Biopolymers 9: 1059-1077.
    • (1970) Biopolymers , vol.9 , pp. 1059-1077
    • Cantor, C.R.1    Warshaw, M.M.2    Shapiro, H.3
  • 15
    • 33751385449 scopus 로고
    • Vibrational motions of bases of nucleic acids as revealed by neutron inelastic scattering and resonance Raman spectroscopy: 1. Adenine and its deuterated species
    • Dhaouadi Z, Ghomi M, Austin JC, Girling RB, Hester RE, Mojzes P, Chinsky L, Turpin PY, Coulombeau C, Jobic H, et al. 1993. Vibrational motions of bases of nucleic acids as revealed by neutron inelastic scattering and resonance Raman spectroscopy: 1. Adenine and its deuterated species. J Phys Chem 97: 1074-1084.
    • (1993) J Phys Chem , vol.97 , pp. 1074-1084
    • Dhaouadi, Z.1    Ghomi, M.2    Austin, J.C.3    Girling, R.B.4    Hester, R.E.5    Mojzes, P.6    Chinsky, L.7    Turpin, P.Y.8    Coulombeau, C.9    Jobic, H.10
  • 19
    • 0000494966 scopus 로고    scopus 로고
    • 2,6-Di(heteroarylvinyl)-pyridines as new potential antitumor agents
    • Fichera M, Gregoli L, Musumarra G. 2000. 2,6-Di(heteroarylvinyl)- pyridines as new potential antitumor agents. J Phys Org Chem 13: 344-346.
    • (2000) J Phys Org Chem , vol.13 , pp. 344-346
    • Fichera, M.1    Gregoli, L.2    Musumarra, G.3
  • 20
    • 0032808969 scopus 로고    scopus 로고
    • Polyamine-based chemotherapy of cancer
    • Frydman B, Valasinas A. 1999. Polyamine-based chemotherapy of cancer. Exp Opin Ther Patents 9: 1055-1068.
    • (1999) Exp Opin Ther Patents , vol.9 , pp. 1055-1068
    • Frydman, B.1    Valasinas, A.2
  • 21
    • 0025572739 scopus 로고
    • 2]spermidine binding to tRNA and to Escherichia coli macromolecules
    • 2]spermidine binding to tRNA and to Escherichia coli macromolecules. J Biol Chem 265: 20874-20878.
    • (1990) J Biol Chem , vol.265 , pp. 20874-20878
    • Frydman, B.1    De Los Santos, C.2    Frydman, R.B.3
  • 26
    • 0017238490 scopus 로고
    • Compact form of DNA induced by spermidine
    • Gosule LC, Schellman JA. 1976. Compact form of DNA induced by spermidine. Nature 259: 333-335.
    • (1976) Nature , vol.259 , pp. 333-335
    • Gosule, L.C.1    Schellman, J.A.2
  • 29
    • 0032127813 scopus 로고    scopus 로고
    • A binding shift assay for the zinc-bound and zinc-free HIV-1 nucleocapsid protein by capillary electrophoresis
    • Guszcynski T, Copeland TD. 1998. A binding shift assay for the zinc-bound and zinc-free HIV-1 nucleocapsid protein by capillary electrophoresis. Anal Biochem 260: 212-217.
    • (1998) Anal Biochem , vol.260 , pp. 212-217
    • Guszcynski, T.1    Copeland, T.D.2
  • 30
    • 57749119521 scopus 로고    scopus 로고
    • Selective structural change by spermidine in the bulged-out region of double-stranded RNA and its effect on RNA function
    • Higashi K, Terui Y, Suganami A, Tamura Y, Nishimura K, Kashiwagi K, Igarashi K. 2008. Selective structural change by spermidine in the bulged-out region of double-stranded RNA and its effect on RNA function. J Biol Chem 283: 32989-32994.
    • (2008) J Biol Chem , vol.283 , pp. 32989-32994
    • Higashi, K.1    Terui, Y.2    Suganami, A.3    Tamura, Y.4    Nishimura, K.5    Kashiwagi, K.6    Igarashi, K.7
  • 32
    • 32944472627 scopus 로고    scopus 로고
    • Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines
    • DOI 10.1093/jb/mvj020
    • Igarashi K, Kashiwagi K. 2006. Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines. J Biochem 139: 11-16. (Pubitemid 43258841)
    • (2006) Journal of Biochemistry , vol.139 , Issue.1 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 34
    • 0031570344 scopus 로고    scopus 로고
    • Solution structure of a metal-binding site in the major groove of RNA complexed with cobalt(III)hexamine
    • Kieft JS, Tinoco I Jr. 1997. Solution structure of a metal-binding site in the major groove of RNA complexed with cobalt(III)hexamine. Structure 5: 713-721.
    • (1997) Structure , vol.5 , pp. 713-721
    • Kieft, J.S.1    Tinoco Jr., I.2
  • 35
    • 0020490025 scopus 로고
    • Numbers of receptor sites from Scatchard graphs: Facts and fantasies
    • Klotz MI. 1982. Numbers of receptor sites from Scatchard graphs: Facts and fantasies. Science 217: 1247-1249.
    • (1982) Science , vol.217 , pp. 1247-1249
    • Klotz, M.I.1
  • 36
    • 33747348387 scopus 로고    scopus 로고
    • Unraveling new features of clindamycin interaction with functional ribosomes and dependence of the drug potency on polyamines
    • DOI 10.1074/jbc.M603263200
    • Kouvela EC, Petropoloulos AD, Kalpaxis DL. 2006. Unraveling new features of clindamycin interaction with functional ribosomes and dependence of the drug potency on polyamines. J Biol Chem 281: 23103-23110. (Pubitemid 44242342)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.32 , pp. 23103-23110
    • Kouvela, E.C.1    Petropoulos, A.D.2    Kalpaxis, D.L.3
  • 37
    • 0030028138 scopus 로고    scopus 로고
    • Synthesis and antitumor evaluation of a highly potent cytotoxic DNA cross-linking polyamine analogue, 1,12-diaziridinyl-4,9-diazadodecane
    • Li Y, Eiseman JL, Sentz DL, Rogers FA, Pan SS, Hu L-T, Egorin MJ, Callery PS. 1996. Synthesis and antitumor evaluation of a highly potent cytotoxic DNA cross-linking polyamine analogue, 1,12-diaziridinyl-4,9-diazadodecane. J Med Chem 39: 339-341. (Pubitemid 126590461)
    • (1996) Journal of Medicinal Chemistry , vol.39 , Issue.1 , pp. 339-341
    • Li, Y.1    Eiseman, J.L.2    Sentz, D.L.3    Rogers, F.A.4    Pan, S.-S.5    Hu, L.-T.6    Egorin, M.J.7    Callery, P.S.8
  • 38
    • 85010439719 scopus 로고
    • A procedure for isolation of deoxyribonucleic acid from micro-organisms
    • Marmur J. 1961. A procedure for isolation of deoxyribonucleic acid from micro-organisms. J Mol Biol 3: 208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 39
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton LJ, Pegg AE. 1995. Polyamines as targets for therapeutic intervention. Annu Rev Pharmacol Toxicol 35: 55-91.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 44
    • 0008875663 scopus 로고
    • Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA
    • Quigley GJ, Teeter MM, Rich A. 1978. Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc Natl Acad Sci 75: 64-68.
    • (1978) Proc Natl Acad Sci , vol.75 , pp. 64-68
    • Quigley, G.J.1    Teeter, M.M.2    Rich, A.3
  • 45
    • 0034602926 scopus 로고    scopus 로고
    • Solution structure of cobalt(III)hexammine complexed to the GAAA tetraloop, and metal-ion binding to G·A mismatches
    • Rüdisser S, Tinoco I Jr. 1999. Solution structure of cobalt(III)hexammine complexed to the GAAA tetraloop, and metal-ion binding to G·A mismatches. J Mol Biol 295: 1211-1223.
    • (1999) J Mol Biol , vol.295 , pp. 1211-1223
    • Rüdisser, S.1    Tinoco Jr., I.2
  • 46
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1. 93 å resolution. A classic structure revisited
    • Shi H, Moore PB. 2000. The crystal structure of yeast phenylalanine tRNA at 1. 93 Å resolution. A classic structure revisited. RNA 6: 1091-1105.
    • (2000) RNA , vol.6 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 47
    • 0030601063 scopus 로고    scopus 로고
    • Spermidine regulation of protein synthesis at the level of initiation complex formation of Met-tRNA, mRNA and ribosomes
    • Shimogori T, Kashiwagi K, Igarashi K. 1996. Spermidine regulation of protein synthesis at the level of initiation complex formation of Met-tRNA, mRNA and ribosomes. Biochem Biophys Res Commun 223: 544-548.
    • (1996) Biochem Biophys Res Commun , vol.223 , pp. 544-548
    • Shimogori, T.1    Kashiwagi, K.2    Igarashi, K.3
  • 48
    • 0018077590 scopus 로고
    • Crystal structure of yeast phenylalanine transfer RNA: I. Crystallographic refinement
    • Sussman JL, Holbrook SR, Warrant RW, Church GM, Kim S-H. 1978. Crystal structure of yeast phenylalanine transfer RNA: I. Crystallographic refinement. J Mol Biol 123: 607-630.
    • (1978) J Mol Biol , vol.123 , pp. 607-630
    • Sussman, J.L.1    Holbrook, S.R.2    Warrant, R.W.3    Church, G.M.4    Kim, S.-H.5
  • 51
    • 0343560974 scopus 로고
    • Structural transitions in DNA (A, B, Z) studied by IR spectroscopy
    • ed. C Sandorfy, T Theophanides, Reidel Dordrecht, Amsterdam
    • Taillandier E, Liquier J, Taboury JA, Ghomi M. 1984a. Structural transitions in DNA (A, B, Z) studied by IR spectroscopy. In Spectroscopy of biological molecules (ed. C Sandorfy, T Theophanides), pp.171-189. Reidel Dordrecht, Amsterdam.
    • (1984) Spectroscopy of Biological Molecules , pp. 171-189
    • Taillandier, E.1    Liquier, J.2    Taboury, J.A.3    Ghomi, M.4
  • 52
    • 0021715186 scopus 로고
    • Left-handed helical structure of polyd(A-C)·poly[d(G-T)] studied by infrared spectroscopy
    • Taillandier E, Taboury JA, Adam S, Liquier J. 1984b. Left-handed helical structure of poly[d(A-C)·poly[d(G-T)] studied by infrared spectroscopy. Biochemistry 23: 5703-5706.
    • (1984) Biochemistry , vol.23 , pp. 5703-5706
    • Taillandier, E.1    Taboury, J.A.2    Adam, S.3    Liquier, J.4
  • 54
    • 0021874218 scopus 로고
    • Flexibility of DNA and RNA upon binding to different metal cations. An investigation of the B to a to Z conformational transition by Fourier Transform Infrared spectroscopy
    • Theophanides T, Tajmir-Riahi HA. 1985. Flexibility of DNA and RNA upon binding to different metal cations. An investigation of the B to A to Z conformational transition by Fourier transform infrared spectroscopy. J Biomol Struct Dyn 2: 995-1004. (Pubitemid 15069020)
    • (1985) Journal of Biomolecular Structure and Dynamics , vol.2 , Issue.5 , pp. 995-1004
    • Theophanides, T.1    Tajmir-Riahi, H.A.2
  • 55
    • 0035099627 scopus 로고    scopus 로고
    • Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications
    • Thomas T, Thomas TJ. 2001. Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications. Cell Mol Life Sci 58: 244-258. (Pubitemid 32217356)
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.2 , pp. 244-258
    • Thomas, T.1    Thomas, T.J.2
  • 56
    • 0141798673 scopus 로고    scopus 로고
    • Polyamine metabolism and cancer
    • Thomas T, Thomas TJ. 2003. Polyamine metabolism and cancer. J Cell Mol Med 7: 113-126.
    • (2003) J Cell Mol Med , vol.7 , pp. 113-126
    • Thomas, T.1    Thomas, T.J.2
  • 58
    • 0014926004 scopus 로고
    • Application of infrared spectroscopy to structure studies of nucleic acids
    • Tsuboi M. 1970. Application of infrared spectroscopy to structure studies of nucleic acids. Appl Spectrosc Rev 3: 45-90.
    • (1970) Appl Spectrosc Rev , vol.3 , pp. 45-90
    • Tsuboi, M.1
  • 59
    • 0025786779 scopus 로고
    • Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver
    • Watanabe S, Kusama-Eguchi K, Kobayashi H, Igarashi K. 1991. Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver. J Biol Chem 266: 20803-20809.
    • (1991) J Biol Chem , vol.266 , pp. 20803-20809
    • Watanabe, S.1    Kusama-Eguchi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 60
    • 0033529644 scopus 로고    scopus 로고
    • Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon aug in OppA mRNA
    • DOI 10.1074/jbc.274.32.22723
    • Yoshida M, Meksuriyen D, Kashiwagi K, Kawai G, Igarashi K. 1999. Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon AUG in oppa mRNA. J Biol Chem 274: 22723-22728. (Pubitemid 29379320)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.32 , pp. 22723-22728
    • Yoshida, M.1    Meksuriyen, D.2    Kashiwagi, K.3    Kawai, G.4    Igarashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.