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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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3394778/
https://www.ncbi.nlm.nih.gov/pubmed/22808041
http://dx.doi.org/10.1371/journal.pone.0039511
Descripción
Sumario: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.

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