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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| Veröffentlicht in: | PloS one 2012-07, Vol.7 (7), p.e39511-e39511 |
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| creator | 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 |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0039511 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0039511</identifier><identifier>PMID: 22808041</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Animals ; Biology ; Cattle ; Cell cycle ; Cullin Proteins - genetics ; Cullin Proteins - metabolism ; Deoxyribonucleic acid ; DNA ; DNA nucleotidylexotransferase ; DNA Nucleotidylexotransferase - genetics ; DNA Nucleotidylexotransferase - metabolism ; DNA polymerases ; DNA repair ; E coli ; Enzymes ; Escherichia coli ; Feedback, Physiological ; Gene Expression Regulation ; Gene Library ; HeLa Cells ; Humans ; Kinases ; Ligases ; Liver - cytology ; Liver - metabolism ; Lymphoid cells ; Nucleotides ; Plasmids ; Proteasome Endopeptidase Complex - genetics ; Proteasome Endopeptidase Complex - metabolism ; Proteasomes ; Proteins ; Proteolysis ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; Science ; T cells ; Thymus Gland - cytology ; Thymus Gland - metabolism ; Transfection ; Ubiquitin ; Ubiquitin-Conjugating Enzymes - genetics ; Ubiquitin-Conjugating Enzymes - metabolism ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination - genetics ; V(D)J recombination</subject><ispartof>PloS one, 2012-07, Vol.7 (7), p.e39511-e39511</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Maezawa et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Maezawa et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-b2b7093646fe6a76c774ecaba83599095c45a3e440bdff5d3dd35f1531c566433</citedby><cites>FETCH-LOGICAL-c758t-b2b7093646fe6a76c774ecaba83599095c45a3e440bdff5d3dd35f1531c566433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3394778/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3394778/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22808041$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Maezawa, So</creatorcontrib><creatorcontrib>Fukushima, Rie</creatorcontrib><creatorcontrib>Matsushita, Toyofumi</creatorcontrib><creatorcontrib>Kato, Tomoyoshi</creatorcontrib><creatorcontrib>Takagaki, Yoshiki</creatorcontrib><creatorcontrib>Nishiyama, Yoshihiro</creatorcontrib><creatorcontrib>Ando, Sachiko</creatorcontrib><creatorcontrib>Matsumoto, Takuro</creatorcontrib><creatorcontrib>Kouda, Kousuke</creatorcontrib><creatorcontrib>Hayano, Takahide</creatorcontrib><creatorcontrib>Suzuki, Masahiro</creatorcontrib><creatorcontrib>Koiwai, Kotaro</creatorcontrib><creatorcontrib>Koiwai, Osamu</creatorcontrib><title>Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity</title><title>PloS one</title><addtitle>PLoS One</addtitle><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.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Biology</subject><subject>Cattle</subject><subject>Cell cycle</subject><subject>Cullin Proteins - genetics</subject><subject>Cullin Proteins - metabolism</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA nucleotidylexotransferase</subject><subject>DNA Nucleotidylexotransferase - genetics</subject><subject>DNA Nucleotidylexotransferase - metabolism</subject><subject>DNA polymerases</subject><subject>DNA repair</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Feedback, Physiological</subject><subject>Gene Expression Regulation</subject><subject>Gene Library</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinases</subject><subject>Ligases</subject><subject>Liver - cytology</subject><subject>Liver - metabolism</subject><subject>Lymphoid cells</subject><subject>Nucleotides</subject><subject>Plasmids</subject><subject>Proteasome Endopeptidase Complex - 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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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22808041</pmid><doi>10.1371/journal.pone.0039511</doi><tpages>e39511</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2012-07, Vol.7 (7), p.e39511-e39511 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1325498134 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Animals Biology Cattle Cell cycle Cullin Proteins - genetics Cullin Proteins - metabolism Deoxyribonucleic acid DNA DNA nucleotidylexotransferase DNA Nucleotidylexotransferase - genetics DNA Nucleotidylexotransferase - metabolism DNA polymerases DNA repair E coli Enzymes Escherichia coli Feedback, Physiological Gene Expression Regulation Gene Library HeLa Cells Humans Kinases Ligases Liver - cytology Liver - metabolism Lymphoid cells Nucleotides Plasmids Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism Proteasomes Proteins Proteolysis Repressor Proteins - genetics Repressor Proteins - metabolism Science T cells Thymus Gland - cytology Thymus Gland - metabolism Transfection Ubiquitin Ubiquitin-Conjugating Enzymes - genetics Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination - genetics V(D)J recombination |
| title | Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-18T21%3A47%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ubiquitylation%20of%20terminal%20deoxynucleotidyltransferase%20inhibits%20its%20activity&rft.jtitle=PloS%20one&rft.au=Maezawa,%20So&rft.date=2012-07-11&rft.volume=7&rft.issue=7&rft.spage=e39511&rft.epage=e39511&rft.pages=e39511-e39511&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0039511&rft_dat=%3Cgale_plos_%3EA477113444%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1325498134&rft_id=info:pmid/22808041&rft_galeid=A477113444&rft_doaj_id=oai_doaj_org_article_194234b13831488a80810564216a1aee&rfr_iscdi=true |