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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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
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 |
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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 |
author_facet | 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 |
author_sort | Maezawa, So |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-3394778 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33947782012-07-17 Ubiquitylation of Terminal Deoxynucleotidyltransferase Inhibits Its Activity 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 PLoS One Research Article 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. Public Library of Science 2012-07-11 /pmc/articles/PMC3394778/ /pubmed/22808041 http://dx.doi.org/10.1371/journal.pone.0039511 Text en Maezawa et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article 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 Ubiquitylation of Terminal Deoxynucleotidyltransferase Inhibits Its Activity |
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 |
topic | Research Article |
url | 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 |
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