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ABSTRACT

Terminal deoxynucleotidyltransferase (TdT), which template-independently synthesizes DNA during V(D)J recombination in lymphoid cells, is ubiquitylated by a BPOZ-2/Cul3 complex, as the ubiquitin ligase, and then degraded by the 26 S proteasome. We show here that TdT is ubiquitylated by the Cul3-based ubiquitylation system in vitro. Because TdT could also be ubiquitylated in the absence of Cul/BPOZ-2, we determined that it could also be directly ubiquitylated by the E2 proteins UbcH5a/b/c and UbcH6, E3-independently. Furthermore, the ubiquitylated TdT inhibited its nucleotidyltransferase activity.

Subject(s)

DNA Nucleotidylexotransferase/metabolism , Feedback, Physiological , Gene Expression Regulation , Ubiquitination/genetics , Animals , Cattle , Cullin Proteins/genetics , Cullin Proteins/metabolism , DNA Nucleotidylexotransferase/genetics , Gene Library , HeLa Cells , Humans , Liver/cytology , Liver/metabolism , Plasmids , Proteasome Endopeptidase Complex/genetics , Proteasome Endopeptidase Complex/metabolism , Proteolysis , Repressor Proteins/genetics , Repressor Proteins/metabolism , Thymus Gland/cytology , Thymus Gland/metabolism , Transfection , Ubiquitin-Conjugating Enzymes/genetics , Ubiquitin-Conjugating Enzymes/metabolism , Ubiquitin-Protein Ligases/genetics , Ubiquitin-Protein Ligases/metabolism

ABSTRACT

Subject(s)

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