The cca-end of p-trna contacts both the human rpl36al and the a-site bound translation termination factor erf1 at the peptidyl transferase center of the human 80s ribosome

Open Biochemistry Journal

Volumn 8, Issue , 2014, Pages 52-67

  Hountondji, Codjo ^a   Bulygin, Konstantin ^a,b   Créchet, Jean Bernard ^c   Woisard, Anne ^a   Tuffery, Pierre ^d   Nakayama, Jun Ichi ^e   Frolova, Ludmila ^f   Nierhaus, Knud H ^g   Karpova, Galina ^b   Baouz, Soria ^a  

^a SORBONNE UNIVERSITÉ   (France)

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

^c ECOLE POLYTECHNIQUE   (France)

^d UNIVERSITÉ PARIS DESCARTES   (France)

^e NAGOYA CITY UNIVERSITY   (Japan)

^f ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^g CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

A site stop codon; Abnormally low pK for Lys 53 of human RPL36AL; CCA end; Conformational change of eRF1 upon binding to the ribosome; Crosslinking; Effect of the eRF1 eRF3 complex on the crosslinking of eRF1 in the human 80S ribosome; ERF1; Human s80S ribosomes; P tRNA; Recombinant human RPL36AL; RPL36AL tRNAox eRF1 ternary complex on the human 80S ribosome

Indexed keywords

ALDEHYDE; AMINO ACID TRANSFER RNA LIGASE; GUANOSINE TRIPHOSPHATE; PEPTIDYLTRANSFERASE; PERIODATE SODIUM; PHENYLALANINE TRANSFER RNA; RIBONUCLEASE; TRANSLATION TERMINATION FACTOR;

ARTICLE; ASSOCIATION RATE CONSTANT; BINDING ASSAY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CROSS LINKING; CRYOELECTRON MICROSCOPY; DISSOCIATION RATE CONSTANT; ENZYME ACTIVITY; HALOARCULA MARISMORTUI; HUMAN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE BINDING SITE; NUCLEOTIDE SEQUENCE; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN NUCLEIC ACID INTERACTION; RIBOSOME; RNA TRANSLATION; SIGNAL TRANSDUCTION; STOP CODON; SURFACE PLASMON RESONANCE; X RAY ANALYSIS;

EID: 84928994005     PISSN: None     EISSN: 1874091X     Source Type: Journal    
DOI: 10.2174/1874091X01408010052     Document Type: Article

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