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| Content Provider | PubMed Central |
|---|---|
| Author | 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 |
| Editor | Vertessy, Beata G. |
| Copyright Year | 2012 |
| 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. |
| Related Links | http://dx.doi.org/10.1371/journal.pone.0039511 |
| Starting Page | 39511 |
| File Format | |
| ISSN | 19326203 |
| e-ISSN | 19326203 |
| Journal | PLoS ONE |
| Issue Number | 7 |
| Volume Number | 7 |
| Language | English |
| Publisher | Public Library of Science |
| Publisher Date | 2012-07-11 |
| Access Restriction | Open |
| Rights Holder | Public Library of Science |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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