Diverse modes of regulating methyltransferase activity by histone ubiquitination

Diverse modes of regulating methyltransferase activity by histone ubiquitination

Post-translational modification of histones plays a central role in regulating transcription. Methylation of histone H3 at lysines 4 (H3K4) and 79 (H3K79) play roles in activating transcription whereas methylation of H3K27 is a repressive mark. These modifications, in turn, depend upon prior monoubi...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Current opinion in structural biology 2023-10, Vol.82, p.102649-102649, Article 102649
Hauptverfasser: Fields, James K., Hicks, Chad W., Wolberger, Cynthia
Format: Artikel
Sprache:eng
Schlagworte:
Histones - metabolism
Humans
Methylation
Protein Processing, Post-Translational
Saccharomyces cerevisiae - metabolism
Ubiquitination
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 102649
container_issue
container_start_page 102649
container_title Current opinion in structural biology
container_volume 82
creator Fields, James K.
Hicks, Chad W.
Wolberger, Cynthia
description Post-translational modification of histones plays a central role in regulating transcription. Methylation of histone H3 at lysines 4 (H3K4) and 79 (H3K79) play roles in activating transcription whereas methylation of H3K27 is a repressive mark. These modifications, in turn, depend upon prior monoubiquitination of specific histone residues in a phenomenon known as histone crosstalk. Earlier work had provided insights into the mechanism by which monoubiquitination histone H2BK120 stimulates H3K4 methylation by COMPASS/MLL1 and H3K79 methylation by DOT1L, and monoubiquitinated H2AK119 stimulates methylation of H3K27 by the PRC2 complex. Recent studies have shed new light on the role of individual subunits and paralogs in regulating the activity of PRC2 and how additional post-translational modifications regulate yeast Dot1 and human DOT1L, as well as provided new insights into the regulation of MLL1 by H2BK120ub.
doi_str_mv 10.1016/j.sbi.2023.102649
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10527252</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0959440X23001239</els_id><sourcerecordid>2854434146</sourcerecordid><originalsourceid>FETCH-LOGICAL-c452t-dc5138d11c2222434f50746068138d8b26dcb8d2ac242f3bca2a4ba0801fdc973</originalsourceid><addsrcrecordid>eNp9kUtLAzEUhYMotlZ_gBuZpZupSSbzwoVIfUJBFwrdhUxyp02ZmbRJptB_b0qr6MZsQpLvnBzuQeiS4DHBJLtZjl2lxxTTJJxpxsojNCRFXsY4SWbHaIjLtIwZw7MBOnNuiTHOCCtO0SDJGS0JK4fo_UFvwDqIWqPARaaOLMz7RnjdzaMW_GLbeCs6V4MVgRLS643226jaRgvtvOkg6iu97nUQBJHpztFJLRoHF4d9hD6fHj8mL_H07fl1cj-NJUupj5VMSVIoQiQNiyWsTnHOMpwVu-uiopmSVaGokJTROqmkoIJVAheY1EqWeTJCd3vfVV-1oCR0IWfDV1a3wm65EZr_fen0gs_NhhOc0pymNDhcHxysWffgPG-1k9A0ogPTO06LlIVghGUBJXtUWuOchfrnH4L5rgq-5KEKvquC76sImqvfAX8U37MPwO0egDCmjQbLndTQSVDagvRcGf2P_RcAQJwE</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2854434146</pqid></control><display><type>article</type><title>Diverse modes of regulating methyltransferase activity by histone ubiquitination</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Fields, James K. ; Hicks, Chad W. ; Wolberger, Cynthia</creator><creatorcontrib>Fields, James K. ; Hicks, Chad W. ; Wolberger, Cynthia</creatorcontrib><description>Post-translational modification of histones plays a central role in regulating transcription. Methylation of histone H3 at lysines 4 (H3K4) and 79 (H3K79) play roles in activating transcription whereas methylation of H3K27 is a repressive mark. These modifications, in turn, depend upon prior monoubiquitination of specific histone residues in a phenomenon known as histone crosstalk. Earlier work had provided insights into the mechanism by which monoubiquitination histone H2BK120 stimulates H3K4 methylation by COMPASS/MLL1 and H3K79 methylation by DOT1L, and monoubiquitinated H2AK119 stimulates methylation of H3K27 by the PRC2 complex. Recent studies have shed new light on the role of individual subunits and paralogs in regulating the activity of PRC2 and how additional post-translational modifications regulate yeast Dot1 and human DOT1L, as well as provided new insights into the regulation of MLL1 by H2BK120ub.</description><identifier>ISSN: 0959-440X</identifier><identifier>ISSN: 1879-033X</identifier><identifier>EISSN: 1879-033X</identifier><identifier>DOI: 10.1016/j.sbi.2023.102649</identifier><identifier>PMID: 37429149</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Histones - metabolism ; Humans ; Methylation ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae - metabolism ; Ubiquitination</subject><ispartof>Current opinion in structural biology, 2023-10, Vol.82, p.102649-102649, Article 102649</ispartof><rights>2023 Elsevier Ltd</rights><rights>Copyright © 2023 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-dc5138d11c2222434f50746068138d8b26dcb8d2ac242f3bca2a4ba0801fdc973</citedby><cites>FETCH-LOGICAL-c452t-dc5138d11c2222434f50746068138d8b26dcb8d2ac242f3bca2a4ba0801fdc973</cites><orcidid>0000-0001-5923-108X ; 0000-0001-8578-2969 ; 0000-0002-6040-6227</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.sbi.2023.102649$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37429149$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fields, James K.</creatorcontrib><creatorcontrib>Hicks, Chad W.</creatorcontrib><creatorcontrib>Wolberger, Cynthia</creatorcontrib><title>Diverse modes of regulating methyltransferase activity by histone ubiquitination</title><title>Current opinion in structural biology</title><addtitle>Curr Opin Struct Biol</addtitle><description>Post-translational modification of histones plays a central role in regulating transcription. Methylation of histone H3 at lysines 4 (H3K4) and 79 (H3K79) play roles in activating transcription whereas methylation of H3K27 is a repressive mark. These modifications, in turn, depend upon prior monoubiquitination of specific histone residues in a phenomenon known as histone crosstalk. Earlier work had provided insights into the mechanism by which monoubiquitination histone H2BK120 stimulates H3K4 methylation by COMPASS/MLL1 and H3K79 methylation by DOT1L, and monoubiquitinated H2AK119 stimulates methylation of H3K27 by the PRC2 complex. Recent studies have shed new light on the role of individual subunits and paralogs in regulating the activity of PRC2 and how additional post-translational modifications regulate yeast Dot1 and human DOT1L, as well as provided new insights into the regulation of MLL1 by H2BK120ub.</description><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Methylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Ubiquitination</subject><issn>0959-440X</issn><issn>1879-033X</issn><issn>1879-033X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtLAzEUhYMotlZ_gBuZpZupSSbzwoVIfUJBFwrdhUxyp02ZmbRJptB_b0qr6MZsQpLvnBzuQeiS4DHBJLtZjl2lxxTTJJxpxsojNCRFXsY4SWbHaIjLtIwZw7MBOnNuiTHOCCtO0SDJGS0JK4fo_UFvwDqIWqPARaaOLMz7RnjdzaMW_GLbeCs6V4MVgRLS643226jaRgvtvOkg6iu97nUQBJHpztFJLRoHF4d9hD6fHj8mL_H07fl1cj-NJUupj5VMSVIoQiQNiyWsTnHOMpwVu-uiopmSVaGokJTROqmkoIJVAheY1EqWeTJCd3vfVV-1oCR0IWfDV1a3wm65EZr_fen0gs_NhhOc0pymNDhcHxysWffgPG-1k9A0ogPTO06LlIVghGUBJXtUWuOchfrnH4L5rgq-5KEKvquC76sImqvfAX8U37MPwO0egDCmjQbLndTQSVDagvRcGf2P_RcAQJwE</recordid><startdate>20231001</startdate><enddate>20231001</enddate><creator>Fields, James K.</creator><creator>Hicks, Chad W.</creator><creator>Wolberger, Cynthia</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5923-108X</orcidid><orcidid>https://orcid.org/0000-0001-8578-2969</orcidid><orcidid>https://orcid.org/0000-0002-6040-6227</orcidid></search><sort><creationdate>20231001</creationdate><title>Diverse modes of regulating methyltransferase activity by histone ubiquitination</title><author>Fields, James K. ; Hicks, Chad W. ; Wolberger, Cynthia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-dc5138d11c2222434f50746068138d8b26dcb8d2ac242f3bca2a4ba0801fdc973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Methylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fields, James K.</creatorcontrib><creatorcontrib>Hicks, Chad W.</creatorcontrib><creatorcontrib>Wolberger, Cynthia</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Current opinion in structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fields, James K.</au><au>Hicks, Chad W.</au><au>Wolberger, Cynthia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Diverse modes of regulating methyltransferase activity by histone ubiquitination</atitle><jtitle>Current opinion in structural biology</jtitle><addtitle>Curr Opin Struct Biol</addtitle><date>2023-10-01</date><risdate>2023</risdate><volume>82</volume><spage>102649</spage><epage>102649</epage><pages>102649-102649</pages><artnum>102649</artnum><issn>0959-440X</issn><issn>1879-033X</issn><eissn>1879-033X</eissn><abstract>Post-translational modification of histones plays a central role in regulating transcription. Methylation of histone H3 at lysines 4 (H3K4) and 79 (H3K79) play roles in activating transcription whereas methylation of H3K27 is a repressive mark. These modifications, in turn, depend upon prior monoubiquitination of specific histone residues in a phenomenon known as histone crosstalk. Earlier work had provided insights into the mechanism by which monoubiquitination histone H2BK120 stimulates H3K4 methylation by COMPASS/MLL1 and H3K79 methylation by DOT1L, and monoubiquitinated H2AK119 stimulates methylation of H3K27 by the PRC2 complex. Recent studies have shed new light on the role of individual subunits and paralogs in regulating the activity of PRC2 and how additional post-translational modifications regulate yeast Dot1 and human DOT1L, as well as provided new insights into the regulation of MLL1 by H2BK120ub.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>37429149</pmid><doi>10.1016/j.sbi.2023.102649</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-5923-108X</orcidid><orcidid>https://orcid.org/0000-0001-8578-2969</orcidid><orcidid>https://orcid.org/0000-0002-6040-6227</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0959-440X
ispartof Current opinion in structural biology, 2023-10, Vol.82, p.102649-102649, Article 102649
issn 0959-440X
1879-033X
1879-033X
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10527252
source MEDLINE; Elsevier ScienceDirect Journals
subjects Histones - metabolism
Humans
Methylation
Protein Processing, Post-Translational
Saccharomyces cerevisiae - metabolism
Ubiquitination
title Diverse modes of regulating methyltransferase activity by histone ubiquitination
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T14%3A09%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Diverse%20modes%20of%20regulating%20methyltransferase%20activity%20by%20histone%20ubiquitination&rft.jtitle=Current%20opinion%20in%20structural%20biology&rft.au=Fields,%20James%20K.&rft.date=2023-10-01&rft.volume=82&rft.spage=102649&rft.epage=102649&rft.pages=102649-102649&rft.artnum=102649&rft.issn=0959-440X&rft.eissn=1879-033X&rft_id=info:doi/10.1016/j.sbi.2023.102649&rft_dat=%3Cproquest_pubme%3E2854434146%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2854434146&rft_id=info:pmid/37429149&rft_els_id=S0959440X23001239&rfr_iscdi=true