Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity

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-base...

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Veröffentlicht in:	PloS one 2012-07, Vol.7 (7), p.e39511-e39511
Hauptverfasser:	Maezawa, So, Fukushima, Rie, Matsushita, Toyofumi, Kato, Tomoyoshi, Takagaki, Yoshiki, Nishiyama, Yoshihiro, Ando, Sachiko, Matsumoto, Takuro, Kouda, Kousuke, Hayano, Takahide, Suzuki, Masahiro, Koiwai, Kotaro, Koiwai, Osamu
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Animals Biology Cattle Cell cycle Cullin Proteins - genetics Cullin Proteins - metabolism Deoxyribonucleic acid DNA DNA nucleotidylexotransferase DNA Nucleotidylexotransferase - genetics DNA Nucleotidylexotransferase - metabolism DNA polymerases DNA repair E coli Enzymes Escherichia coli Feedback, Physiological Gene Expression Regulation Gene Library HeLa Cells Humans Kinases Ligases Liver - cytology Liver - metabolism Lymphoid cells Nucleotides Plasmids Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism Proteasomes Proteins Proteolysis Repressor Proteins - genetics Repressor Proteins - metabolism Science T cells Thymus Gland - cytology Thymus Gland - metabolism Transfection Ubiquitin Ubiquitin-Conjugating Enzymes - genetics Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination - genetics V(D)J recombination
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