A translation system reconstituted with human factors proves that processing of encephalomyocarditis virus proteins 2A and 2B occurs in the elongation phase of translation without eukaryotic release factors

Journal of Biological Chemistry

Volumn 289, Issue 46, 2014, Pages 31960-31971

  Machida, Kodai ^a   Mikami, Satoshi ^b   Masutani, Mamiko ^a   Mishima, Kurumi ^a   Kobayashi, Tominari ^a,c   Imataka, Hiroaki ^a  

^a UNIVERSITY OF HYOGO   (Japan)

^b RIKEN   (Japan)

^c JICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN ENGINEERING; PROTEINS; VIRUSES;

ENCEPHALOMYOCARDITIS VIRUS; EUKARYOTIC PROTEIN SYNTHESIS; RELEASE FACTORS; TRANSLATION SYSTEMS;

BIOSYNTHESIS;

AMINO ACID TRANSFER RNA LIGASE; CELL PROTEIN; ELONGATION FACTOR; EUKARYOTIC ELONGATION FACTOR 1; EUKARYOTIC ELONGATION FACTOR 2; EUKARYOTIC RELEASE FACTOR 1; EUKARYOTIC RELEASE FACTOR 3; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 2A; NONSTRUCTURAL PROTEIN 2B; TRANSFER RNA; UNCLASSIFIED DRUG; ALANINE; COMPLEMENTARY DNA; ELONGATION FACTOR 1; INITIATION FACTOR 2; VIRUS PROTEIN; VIRUS PROTEIN 2A;

ARTICLE; ENCEPHALOMYOCARDITIS VIRUS; EUKARYOTE; HEPATITIS C VIRUS; IN VITRO STUDY; INTERNAL RIBOSOME ENTRY SITE; NONHUMAN; PLASMID; PROKARYOTE; PROTEIN CLEAVAGE; PROTEIN PROCESSING; PROTEIN SUBUNIT; PROTEIN SYNTHESIS; RIBOSOME; RNA TRANSLATION; BINDING SITE; CELL FREE SYSTEM; CHEMISTRY; GENE DELETION; GENE EXPRESSION REGULATION; GENETICS; HELA CELL LINE; HEPACIVIRUS; HUMAN; METABOLISM; MUTATION; OPEN READING FRAME; PROTEIN FOLDING;

ENCEPHALOMYOCARDITIS VIRUS; EUKARYOTA;

ALANINE; AMINO ACYL-TRNA SYNTHETASES; BINDING SITES; CELL-FREE SYSTEM; DNA, COMPLEMENTARY; ENCEPHALOMYOCARDITIS VIRUS; EUKARYOTIC INITIATION FACTOR-2; GENE DELETION; GENE EXPRESSION REGULATION; HELA CELLS; HEPACIVIRUS; HUMANS; MUTATION; OPEN READING FRAMES; PEPTIDE ELONGATION FACTOR 1; PLASMIDS; PROTEIN BIOSYNTHESIS; PROTEIN FOLDING; RIBOSOMES; VIRAL NONSTRUCTURAL PROTEINS; VIRAL PROTEINS;

EID: 84911095696     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.593343     Document Type: Article

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