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. 1987 Jul 24;15(14):5787–5801. doi: 10.1093/nar/15.14.5787

Crosslinking of elongation factor Tu to tRNA(Phe) by trans-diamminedichloroplatinum (II). Characterization of two crosslinking sites in the tRNA.

F P Wikman, P Romby, M H Metz, J Reinbolt, B F Clark, J P Ebel, C Ehresmann, B Ehresmann
PMCID: PMC306023  PMID: 3302946

Abstract

Trans-diamminedichloroplatinum (II) was used to induce reversible crosslinks between EF-Tu and Phe-tRNA(Phe) within the ternary EF-Tu/GTP/Phe-tRNA(Phe) complex. Up to 40% of the complex was specifically converted into crosslinked species. Two crosslinking sites have been unambiguously identified. The major one encompassing nucleotides 58 to 65 is located in the 3'-part of the T-stem, and the minor one encompassing nucleotides 31 to 42 includes the anticodon loop and part of the 3'-strand of the anticodon stem.

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Selected References

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  1. Antonsson B., Leberman R., Jacrot B., Zaccai G. Small-angle neutron scattering study of the ternary complex formed between bacterial elongation factor Tu, guanosine 5'-triphosphate, and valyl-tRNAVal. Biochemistry. 1986 Jun 17;25(12):3655–3659. doi: 10.1021/bi00360a027. [DOI] [PubMed] [Google Scholar]
  2. Antonsson B., Leberman R. Modification of amino groups in EF-Tu.GTP and the ternary complex EF-Tu.GTP.valyl-tRNAVal. Eur J Biochem. 1984 Jun 15;141(3):483–487. doi: 10.1111/j.1432-1033.1984.tb08218.x. [DOI] [PubMed] [Google Scholar]
  3. Boutorin A. S., Clark B. F., Ebel J. P., Kruse T. A., Petersen H. U., Remy P., Vassilenko S. A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease. J Mol Biol. 1981 Nov 5;152(3):593–608. doi: 10.1016/0022-2836(81)90271-0. [DOI] [PubMed] [Google Scholar]
  4. Dirheimer G., Ebel J. P. Fractionnement des tRNA de levure de bière par distribution en contre-courant. Bull Soc Chim Biol (Paris) 1967;49(12):1679–1687. [PubMed] [Google Scholar]
  5. Douthwaite S., Garrett R. A., Wagner R. Comparison of Escherichia coli tRNAPhe in the free state, in the ternary complex and in the ribosomal A and P sites by chemical probing. Eur J Biochem. 1983 Mar 15;131(2):261–269. doi: 10.1111/j.1432-1033.1983.tb07258.x. [DOI] [PubMed] [Google Scholar]
  6. Ehresmann C., Moine H., Mougel M., Dondon J., Grunberg-Manago M., Ebel J. P., Ehresmann B. Cross-linking of initiation factor IF3 to Escherichia coli 30S ribosomal subunit by trans-diamminedichloroplatinum(II): characterization of two cross-linking sites in 16S rRNA; a possible way of functioning for IF3. Nucleic Acids Res. 1986 Jun 25;14(12):4803–4821. doi: 10.1093/nar/14.12.4803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fischer W., Doi T., Ikehara M., Ohtsuka E., Sprinzl M. Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu. FEBS Lett. 1985 Nov 11;192(1):151–154. doi: 10.1016/0014-5793(85)80062-4. [DOI] [PubMed] [Google Scholar]
  8. Garrett-Wheeler E., Lockard R. E., Kumar A. Mapping of psoralen cross-linked nucleotides in RNA. Nucleic Acids Res. 1984 Apr 11;12(7):3405–3423. doi: 10.1093/nar/12.7.3405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hansen P. K., Wikman F., Clark B. F., Hershey J. W., Uffe Petersen H. Interaction between initiator Met-tRNAfMet and elongation factor EF-Tu from E. coli. Biochimie. 1986 May;68(5):697–703. doi: 10.1016/s0300-9084(86)80163-8. [DOI] [PubMed] [Google Scholar]
  10. Jack A., Ladner J. E., Rhodes D., Brown R. S., Klug A. A crystallographic study of metal-binding to yeast phenylalanine transfer RNA. J Mol Biol. 1977 Apr 15;111(3):315–328. doi: 10.1016/s0022-2836(77)80054-5. [DOI] [PubMed] [Google Scholar]
  11. Jekowsky E., Schimmel P. R., Miller D. L. Isolation, characterization and structural implications of a nuclease-digested complex of aminoacyl transfer RNA and Escherichia coli elongation factor Tu. J Mol Biol. 1977 Aug 15;114(3):451–458. doi: 10.1016/0022-2836(77)90262-5. [DOI] [PubMed] [Google Scholar]
  12. Kabsch W., Gast W. H., Schulz G. E., Leberman R. Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli. J Mol Biol. 1977 Dec 25;117(4):999–1012. doi: 10.1016/s0022-2836(77)80009-0. [DOI] [PubMed] [Google Scholar]
  13. Kao T., Miller D. L., Abo M., Ofengand J. Formation and properties of a covalent complex between elongation factor Tu and Phe-tRNA bearing a photoaffinity probe on its 3-(3-amino-3-carboxypropyl)uridine residue. J Mol Biol. 1983 May 25;166(3):383–405. doi: 10.1016/s0022-2836(83)80091-6. [DOI] [PubMed] [Google Scholar]
  14. Kern D., Dietrich A., Fasiolo F., Renaud M., Giegé R., Ebel J. P. The yeast aminoacyl-tRNA synthetases. Methodology for their complete or partial purification and comparison of their relative activities under various extraction conditions. Biochimie. 1977;59(5-6):453–462. doi: 10.1016/s0300-9084(77)80050-3. [DOI] [PubMed] [Google Scholar]
  15. Kern D., Giegé R., Robre-Saul S., Boulanger Y., Ebel J. P. Complete purification and studies on the structural and kinetic properties of two forms of yeast valyl-tRNA synthetase. Biochimie. 1975;57(10):1167–1176. doi: 10.1016/s0300-9084(76)80579-2. [DOI] [PubMed] [Google Scholar]
  16. Louie A., Jurnak F. Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes. Biochemistry. 1985 Nov 5;24(23):6433–6439. doi: 10.1021/bi00344a019. [DOI] [PubMed] [Google Scholar]
  17. Louie A., Ribeiro N. S., Reid B. R., Jurnak F. Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP. J Biol Chem. 1984 Apr 25;259(8):5010–5016. [PubMed] [Google Scholar]
  18. Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Osterberg R., Elias P., Kjems J., Bauer R. A neutron scattering study of the ternary complex EF-Tu.GTP-valyl-tRNAVal1A. J Biomol Struct Dyn. 1986 Jun;3(6):1111–1120. doi: 10.1080/07391102.1986.10508488. [DOI] [PubMed] [Google Scholar]
  20. Osterberg R., Sjöberg B., Ligaarden R., Elias P. A small-angle X-ray scattering study of the complex formation between elongation factor Tu . GTP and valyl-tRNA Val I from Escherichia coli. Eur J Biochem. 1981 Jun;117(1):155–159. doi: 10.1111/j.1432-1033.1981.tb06314.x. [DOI] [PubMed] [Google Scholar]
  21. Pingoud A., Urbanke C., Krauss G., Peters F., Maass G. Ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA: an equilibrium study. Eur J Biochem. 1977 Sep;78(2):403–409. doi: 10.1111/j.1432-1033.1977.tb11752.x. [DOI] [PubMed] [Google Scholar]
  22. Quigley G. J., Seeman N. C., Wang A. H., Suddath F. L., Rich A. Yeast phenylalanine transfer RNA: atomic coordinates and torsion angles. Nucleic Acids Res. 1975 Dec;2(12):2329–2341. doi: 10.1093/nar/2.12.2329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Riehl N., Giegé R., Ebel J. P., Ehresmann B. Effect of elongation factor Tu on the conformation of phenylalanyl-tRNAPhe. FEBS Lett. 1983 Apr 5;154(1):42–46. doi: 10.1016/0014-5793(83)80871-0. [DOI] [PubMed] [Google Scholar]
  24. Rubin J. R., Sabat M., Sundaralingam M. Similar binding of the carcinostatic drugs cis-[Pt(NH3)2Cl2] and [Ru(NH3)5Cl] Cl2 to tRNAphe and a comparison with the binding of the inactive trans-[Pt(NH3)2Cl2] complex - reluctance in binding to Watson-Crick base pairs within double helix. Nucleic Acids Res. 1983 Sep 24;11(18):6571–6586. doi: 10.1093/nar/11.18.6571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Silberklang M., Gillum A. M., RajBhandary U. L. The use of nuclease P1 in sequence analysis of end group labeled RNA. Nucleic Acids Res. 1977 Dec;4(12):4091–4108. doi: 10.1093/nar/4.12.4091. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Weygand-Durasevic I., Kruse T. A., Clark B. F. The influence of elongation-factor-Tu . GTP and anticodon-anticodon interactions on the anticodon loop conformation of yeast tRNATyr. Eur J Biochem. 1981 May;116(1):59–65. doi: 10.1111/j.1432-1033.1981.tb05300.x. [DOI] [PubMed] [Google Scholar]
  27. Wikman F. P., Siboska G. E., Petersen H. U., Clark B. F. The site of interaction of aminoacyl-tRNA with elongation factor Tu. EMBO J. 1982;1(9):1095–1100. doi: 10.1002/j.1460-2075.1982.tb01302.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

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