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

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

Peña, Maria Marjorette O; Melo, Sandra P; Xing, Yang-Yang; White, Kenneth; Barbour, Karen W; Berger, Franklin G.

Affiliation

Peña MM; Department of Biological Sciences, University of South Carolina, Columbia, South Carolina 29208, USA.

J Biol Chem ; 284(46): 31597-607, 2009 Nov 13.

Article in En | MEDLINE | ID: mdl-19797058

Subject(s)

Proteasome Endopeptidase Complex/metabolism; Protein Processing, Post-Translational; Thymidylate Synthase/chemistry; Thymidylate Synthase/metabolism; Ubiquitin/metabolism; Acetylation; Amino Acid Sequence; Animals; Cells, Cultured; Cricetinae; Cricetulus; Electrophoresis, Gel, Two-Dimensional; Fibroblasts/enzymology; Humans; Immunoblotting; Lung/cytology; Lung/enzymology; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thymidylate Synthase/genetics

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Thymidylate Synthase / Protein Processing, Post-Translational / Ubiquitin / Proteasome Endopeptidase Complex Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 2009 Document type: Article Affiliation country: United States Country of publication: United States

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google