Lys53 of Ribosomal Protein L36AL and the CCA End of a tRNA at the P/E Hybrid Site Are in Close Proximity on the Human Ribosome

ChemBioChem

Volumn 13, Issue 12, 2012, Pages 1791-1797

  Hountondji, Codjo ^a   Bulygin, Konstantin ^a,b   Woisard, Anne ^a   Tuffery, Pierre ^c   Créchet, Jean Bernard ^d   Pech, Markus ^e,f   Nierhaus, Knud H ^e,f   Karpova, Galina ^b   Baouz, Soria ^a  

^a SORBONNE UNIVERSITÉ   (France)

^b INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

^c INSERM   (France)

^d INSTITUT DE CHIMIE DES SUBSTANCES NATURELLES   (France)

^e MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^f CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

80S ribosomes; CCA end; Crosslinking; RNA structures; TRNA

Indexed keywords

ARGININE; GLUTAMINE; LYSINE; RIBOSOME PROTEIN; TRANSFER RNA;

AFFINITY LABELING; ARTICLE; CHEMICAL MODIFICATION; CONTROLLED STUDY; CROSS LINKING; EUKARYOTE; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN MOTIF; RIBOSOME; RNA BINDING;

AMINO ACID MOTIFS; ANIMALS; BINDING SITES; CATTLE; CROSS-LINKING REAGENTS; HUMANS; LYSINE; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; RIBOSOMAL PROTEINS; RIBOSOMES; RNA, TRANSFER, AMINO ACYL; SACCHAROMYCES CEREVISIAE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ARCHAEA; EUKARYOTA; MAMMALIA;

EID: 84864765304     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201200208     Document Type: Article

References (24)

1. M. Pech, K. H. Nierhaus, ChemBioChem 2012, 13, 189-192.
2. P. Nissen, J. Hansen, N. Ban, P. B. Moore, T. A. Steitz, Science 2000, 289, 920-930.
3. R. M. Voorhees, A. Weixlbaumer, D. Loakes, A. C. Kelley, V. Ramakrishnan, Nat. Struct. Mol. Biol. 2009, 16, 528-533.
4. T. M. Schmeing, P. B. Moore, T. A. Steitz, RNA 2003, 9, 1345-1352.
5. S. Klinge, F. Voigts-Hoffmann, M. Leibundgut, S. Arpagaus, N. Ban, Science 2011, 334, 941-948.
6. A. Ben-Shem, N. Garreau de Loubresse, S. Melnikov, L. Jenner, G. Yusupova, M. Yusupov, Science 2011, 334, 1524-1529.
7. S. Baouz, A. Woisard, S. Sinapah, J. P. Le Caer, M. Argentini, K. Bulygin, G. Aguie, C. Hountondji, Biochimie 2009, 91, 1420-1425.
8. C. Hountondji, J. M. Schmitter, C. Beauvallet, S. Blanquet, Biochemistry 1990, 29, 8190-8198.
9. C. Hountondji, G. Fayat, S. Blanquet, Eur. J. Biochem. 1979, 102, 247-250.
10. C. Hountondji, G. Fayat, S. Blanquet, Eur. J. Biochem. 1980, 107, 403-407.
11. S. Schilling-Bartetzko, F. Franceschi, H. Sternbach, K. H. Nierhaus, J. Biol. Chem. 1992, 267, 4693-4702.
12. A. Gnirke, K. H. Nierhaus, J. Biol. Chem. 1986, 261, 14506-14514.
13. P. N. Lowe, R. B. Beechey, Biochemistry 1982, 21, 4073-4082.
14. S. B. Easterbrook-Smith, J. C. Wallace, D. B. Keech, Eur. J. Biochem. 1976, 62, 125-130.
15. S. Baouz, J. M. Schmitter, L. Chenoune, C. Beauvallet, S. Blanquet, A. Woisard, C. Hountondji, Open Biochem. J. 2009, 3, 26-38.
16. K. J. Webb, A. Laganowsky, J. P. Whitelegge, S. G. Clarke, J. Biol. Chem. 2008, 283, 35561-35568.
17. A. Shirai, M. Sadaie, K. Shinmyozu, J. Nakayama, J. Biol. Chem. 2010, 285, 22448-22460.
18. V. Heurgue-Hamard, S. Champ, L. Mora, T. Merkulova-Rainon, L. L. Kisselev, R. H. Buckingham, J. Biol. Chem. 2005, 280, 2439-2445.
19. T. Budkevich, J. Giesebrecht, R. B. Altman, J. B. Munro, T. Mielke, K. H. Nierhaus, S. C. Blanchard, C. M. Spahn, Mol. Cell 2011, 44, 214-224.
20. J. B. Munro, R. B. Altman, N. O'Connor, S. C. Blanchard, Mol. Cell 2007, 25, 505-517.
21. N. B. Matasova, S. V. Myltseva, M. A. Zenkova, D. M. Graifer, S. N. Vladimirov, G. G. Karpova, Anal. Biochem. 1991, 198, 219-223.
22. G. Chinali, A. Parmeggiani, Eur. J. Biochem. 1973, 32, 463-472.
23. J. B. Crechet, A. Parmeggiani, Eur. J. Biochem. 1986, 161, 647-653.
24. J. B. Crechet, D. Canceill, V. Bocchini, A. Parmeggiani, Eur. J. Biochem. 1986, 161, 635-645.