PLoS ONE (Jan 2012)

Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity.

  • So Maezawa,
  • Rie Fukushima,
  • Toyofumi Matsushita,
  • Tomoyoshi Kato,
  • Yoshiki Takagaki,
  • Yoshihiro Nishiyama,
  • Sachiko Ando,
  • Takuro Matsumoto,
  • Kousuke Kouda,
  • Takahide Hayano,
  • Masahiro Suzuki,
  • Kotaro Koiwai,
  • Osamu Koiwai

DOI
https://doi.org/10.1371/journal.pone.0039511
Journal volume & issue
Vol. 7, no. 7
p. e39511

Abstract

Read online

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.