The intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathway

Journal of Biological Chemistry

Volumn 284, Issue 46, 2009, Pages 31597-31607

  Peña, Maria Marjorette O ^a   Melo, Sandra P ^a   Xing, Yang Yang ^a   White, Kenneth ^a   Barbour, Karen W ^a   Berger, Franklin G ^a  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHETIC ENZYMES; COMPARATIVE ANALYSIS; DNA REPLICATIONS; EUKARYOTIC CELLS; FREE AMINO GROUPS; HETEROLOGOUS PROTEINS; MAMMALIAN SPECIES; MUTANT PROTEINS; N-TERMINAL DOMAINS; N-TERMINALS; PRIMARY SEQUENCES; PROTEASOMAL DEGRADATION; PROTEASOMES; THYMIDYLATE SYNTHASE; UBIQUITIN;

AMINES; ENZYMES; FLUORINE CONTAINING POLYMERS; GROWTH KINETICS; MAMMALS; NUCLEIC ACIDS;

DEGRADATION;

THYMIDYLATE SYNTHASE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL GROWTH; CELL PROLIFERATION; CONTROLLED STUDY; DNA METHYLATION; DNA REPLICATION; ENZYME DEGRADATION; ENZYME STRUCTURE; HUMAN; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN TARGETING;

ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; CELLS, CULTURED; CRICETINAE; CRICETULUS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FIBROBLASTS; HUMANS; IMMUNOBLOTTING; LUNG; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THYMIDYLATE SYNTHASE; UBIQUITIN;

EUKARYOTA; MAMMALIA;

EID: 70450234993     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.038455     Document Type: Article

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