Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

Journal of Biological Chemistry

Volumn 288, Issue 19, 2013, Pages 13917-13928

  Burnett, Benjamin J ^a   Altman, Roger B ^a   Ferrao, Ryan ^b   Alejo, Jose L ^a   Kaur, Navdep ^a   Kanji, Joshua ^a   Blanchard, Scott C ^a,b  

^a Department of Physiology and Biophysics ^*  (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DECAY RATE; ELONGATION FACTOR; ELONGATION FACTOR TU; G PROTEIN; NOVEL FUNCTIONS; NUCLEOTIDE-EXCHANGE FACTOR; TERNARY COMPLEX;

AMINO ACIDS; DECAY (ORGANIC); ESCHERICHIA COLI;

ELONGATION;

AMINOACYL TRANSFER RNA; ELONGATION FACTOR TS; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN SYNTHESIS; QUANTITATIVE ANALYSIS; STEADY STATE;

ELONGATION FACTOR TS; ELONGATION FACTOR TU; G-PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTOR (GEF); PROTEIN SYNTHESIS; TERNARY COMPLEX; TRANSFER RNA (TRNA); TRANSLATION REGULATION;

BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANOSINE TRIPHOSPHATE; KINETICS; MODELS, MOLECULAR; PEPTIDE ELONGATION FACTOR TU; PEPTIDE ELONGATION FACTORS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA, TRANSFER, AMINO ACYL; SPECTROMETRY, FLUORESCENCE;

EID: 84877696590     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.460014     Document Type: Article

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