Cysteine‐Assisted Click‐Chemistry for Proximity‐Driven, Site‐Specific Acetylation of Histones
Post‐translational modifications of histones are essential in the regulation of chromatin structure and function. Among these modifications, lysine acetylation is one of the most established. Earlier studies relied on the use of chromatin containing heterogeneous mixtures of histones acetylated at m...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2022-11, Vol.61 (46), p.e202208543-n/a |
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| creator | Afonso, Cláudia F. Marques, Marta C. António, João P. M. Cordeiro, Carlos Gois, Pedro M. P. Cal, Pedro M. S. D. Bernardes, Gonçalo J. L. |
| description | Post‐translational modifications of histones are essential in the regulation of chromatin structure and function. Among these modifications, lysine acetylation is one of the most established. Earlier studies relied on the use of chromatin containing heterogeneous mixtures of histones acetylated at multiple sites. Differentiating the individual contribution of single acetylation events towards chromatin regulation is thus of great relevance. However, it is difficult to access homogeneous samples of histones, with a single acetylation, in sufficient quantities for such studies. By engineering histone H3 with a cysteine in proximity of the lysine of interest, we demonstrate that conjugation with maleimide‐DBCO followed by a strain‐promoted alkyne‐azide cycloaddition reaction results in the acetylation of a single lysine in a controlled, site‐specific manner. The chemical precision offered by our click‐to‐acetylate approach will facilitate access to and the study of acetylated histones.
We present a proximity‐driven, lysine‐specific acetylation approach to construct precisely acetylated histone proteins. The approach is facilitated by a click reagent equipped with an acetate group donor to acetylate a nearby lysine in a sequence‐controlled manner. |
| doi_str_mv | 10.1002/anie.202208543 |
| format | Article |
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We present a proximity‐driven, lysine‐specific acetylation approach to construct precisely acetylated histone proteins. The approach is facilitated by a click reagent equipped with an acetate group donor to acetylate a nearby lysine in a sequence‐controlled manner.</description><subject>Acetylation</subject><subject>Alkynes</subject><subject>Chromatin</subject><subject>Click Chemistry</subject><subject>Communication</subject><subject>Communications</subject><subject>Conjugation</subject><subject>Cycloaddition</subject><subject>Cysteine</subject><subject>Cysteine Bioconjugation</subject><subject>Histone H3</subject><subject>Histones</subject><subject>Histones - chemistry</subject><subject>Lysine</subject><subject>Lysine - chemistry</subject><subject>Lysine Acetylation</subject><subject>Maleimide</subject><subject>Protein Processing, Post-Translational</subject><subject>Structure-function relationships</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFkctuFDEQRS1ERB6wZYlaYsMiPfGj_dogjZpAIkUBKbC2PO5q4tBjT-yeQO_4BL6RL8GjSYbHhpXtqnOvqnwRek7wjGBMT2zwMKOYUqx4wx6hA8IpqZmU7HG5N4zVUnGyjw5zvim8Ulg8QftMENooLg8QtFMewQf4-f3HPGdfHl3VDt59KYX2Gpalkqaqj6n6kOI3v_TjVDpvkr-DcFxd-XGjvFqB87131dzBOA129DFUsa_OijoGyE_RXm-HDM_uzyP06e3px_asvnj_7rydX9SuEYrV_UIqJhjHrtOMO8pYp8FRSRvBwXJNFxqwlJpYJYTutCpMA5joRiwk9JIdoddb39V6sYTOQRiTHcwq-aVNk4nWm787wV-bz_HOaEUVx7gYvLo3SPF2DXk05QMcDIMNENfZUEkEVopTVdCX_6A3cZ1CWa9QjHJKOaaFmm0pl2LOCfrdMASbTYJmk6DZJVgEL_5cYYc_RFYAvQW--gGm_9iZ-eX56W_zXyo1rJE</recordid><startdate>20221114</startdate><enddate>20221114</enddate><creator>Afonso, Cláudia F.</creator><creator>Marques, Marta C.</creator><creator>António, João P. M.</creator><creator>Cordeiro, Carlos</creator><creator>Gois, Pedro M. P.</creator><creator>Cal, Pedro M. S. D.</creator><creator>Bernardes, Gonçalo J. L.</creator><general>Wiley Subscription Services, Inc</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><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>7TM</scope><scope>K9.</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4228-8834</orcidid><orcidid>https://orcid.org/0000-0001-6594-8917</orcidid></search><sort><creationdate>20221114</creationdate><title>Cysteine‐Assisted Click‐Chemistry for Proximity‐Driven, Site‐Specific Acetylation of Histones</title><author>Afonso, Cláudia F. ; Marques, Marta C. ; António, João P. M. ; Cordeiro, Carlos ; Gois, Pedro M. P. ; Cal, Pedro M. S. D. ; Bernardes, Gonçalo J. 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L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cysteine‐Assisted Click‐Chemistry for Proximity‐Driven, Site‐Specific Acetylation of Histones</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2022-11-14</date><risdate>2022</risdate><volume>61</volume><issue>46</issue><spage>e202208543</spage><epage>n/a</epage><pages>e202208543-n/a</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>Post‐translational modifications of histones are essential in the regulation of chromatin structure and function. Among these modifications, lysine acetylation is one of the most established. Earlier studies relied on the use of chromatin containing heterogeneous mixtures of histones acetylated at multiple sites. Differentiating the individual contribution of single acetylation events towards chromatin regulation is thus of great relevance. However, it is difficult to access homogeneous samples of histones, with a single acetylation, in sufficient quantities for such studies. By engineering histone H3 with a cysteine in proximity of the lysine of interest, we demonstrate that conjugation with maleimide‐DBCO followed by a strain‐promoted alkyne‐azide cycloaddition reaction results in the acetylation of a single lysine in a controlled, site‐specific manner. The chemical precision offered by our click‐to‐acetylate approach will facilitate access to and the study of acetylated histones.
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| subjects | Acetylation Alkynes Chromatin Click Chemistry Communication Communications Conjugation Cycloaddition Cysteine Cysteine Bioconjugation Histone H3 Histones Histones - chemistry Lysine Lysine - chemistry Lysine Acetylation Maleimide Protein Processing, Post-Translational Structure-function relationships |
| title | Cysteine‐Assisted Click‐Chemistry for Proximity‐Driven, Site‐Specific Acetylation of Histones |
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