Protein synthesis elongation factor EF-1α is essential for ubiquitin- dependent degradation of certain N(α)-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu

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

Volumn 91, Issue 16, 1994, Pages 7648-7652

  Gonen, H ^a   Smith, C E ^a   Siegel, N R ^a   Kahana, C ^a   Merrick, W C ^a   Chakraburtty, K ^a   Schwartz, A L ^a   Ciechanover, A ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

N terminally blocked proteins; proteolysis

Indexed keywords

ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE; PEPTIDASE; PROTEIN; UBIQUITIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TARGETING; RABBIT; RETICULOCYTE; SACCHAROMYCES CEREVISIAE;

ACETYLATION; AMINO ACID SEQUENCE; ANIMAL; ESCHERICHIA COLI; GTP-BINDING PROTEINS; HISTONES; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTOR 1; PEPTIDE ELONGATION FACTOR TU; PEPTIDE ELONGATION FACTORS; PEPTIDE HYDROLASES; PROTEINS; RABBITS; RETICULOCYTES; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SPECIES SPECIFICITY; SUPPORT, NON-U.S. GOV'T; UBIQUITINS;

ANIMALIA; BACTERIA (MICROORGANISMS); ORYCTOLAGUS CUNICULUS; PROKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0028136693     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.91.16.7648     Document Type: Article

References (0)