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...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3394778?pdf=render |
| _version_ | 1819181934617559040 |
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| author | 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 |
| author_facet | 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 |
| author_sort | So Maezawa |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T22:38:07Z |
| format | Article |
| id | doaj.art-194234b13831488a80810564216a1aee |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T22:38:07Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-194234b13831488a80810564216a1aee2022-12-21T18:10:15ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0177e3951110.1371/journal.pone.0039511Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity.So MaezawaRie FukushimaToyofumi MatsushitaTomoyoshi KatoYoshiki TakagakiYoshihiro NishiyamaSachiko AndoTakuro MatsumotoKousuke KoudaTakahide HayanoMasahiro SuzukiKotaro KoiwaiOsamu KoiwaiTerminal 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.http://europepmc.org/articles/PMC3394778?pdf=render |
| spellingShingle | 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 Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. PLoS ONE |
| title | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. |
| title_full | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. |
| title_fullStr | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. |
| title_full_unstemmed | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. |
| title_short | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity. |
| title_sort | ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity |
| url | http://europepmc.org/articles/PMC3394778?pdf=render |
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