Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 9, 1996, Pages 4202-4206

  Borowski, Christian ^a   Rodnina, Marina V ^a   Wintermeyer, Wolfgang ^a  

^a UNIVERSITY OF WITTEN HERDECKE   (Germany)

Author keywords

GTPase; Ribosome

Indexed keywords

ELONGATION FACTOR G; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ANTICODON; ARTICLE; DELETION MUTANT; ESCHERICHIA COLI; GENE TRANSLOCATION; HYDROLYSIS; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; RIBOSOME; RNA BINDING;

ANTICODON; ESCHERICHIA COLI; KINETICS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE ELONGATION FACTOR G; PEPTIDE ELONGATION FACTORS; POLY U; POLYMERASE CHAIN REACTION; PUROMYCIN; RECOMBINANT PROTEINS; RIBOSOMES; RNA, MESSENGER; RNA, TRANSFER, AMINO ACYL; RNA, TRANSFER, PHE; SEQUENCE DELETION;

ESCHERICHIA COLI;

EID: 0029994962     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.9.4202     Document Type: Article

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