SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis
Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9-mediated methylation often regulates the stability, sub-cellular localization a...
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| Veröffentlicht in: | Biochimica et biophysica acta. Molecular cell research 2020-02, Vol.1867 (2), p.118611, Article 118611 |
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| container_title | Biochimica et biophysica acta. Molecular cell research |
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| creator | Mahesh, Arun Khan, Mohd. Imran K. Govindaraju, Gayathri Verma, Mamta Awasthi, Sharad Chavali, Pavithra L. Chavali, Sreenivas Rajavelu, Arumugam Dhayalan, Arunkumar |
| description | Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9-mediated methylation often regulates the stability, sub-cellular localization and protein-protein interactions of its substrate proteins. Here, we aimed to identify novel biological processes regulated by SET7/9 by identifying new interaction partners. For this we used yeast two-hybrid screening and identified the large subunit ribosomal protein, eL42 as a potential interactor of SET7/9. We confirmed the SET7/9-eL42 interaction by co-immunoprecipitation and GST pulldown studies. The N-terminal MORN domain of SET7/9 is essential for its interaction with eL42. Importantly, we identified that SET7/9 methylates eL42 at three different lysines - Lys53, Lys80 and Lys100 through site-directed mutagenesis. By puromycin incorporation assay, we find that SET7/9-mediated methylation of eL42 affects global translation. This study identifies a new role of the functionally versatile SET7/9 lysine methyltransferase in the regulation of global protein synthesis.
[Display omitted]
•Little is known about the regulation and functional significance of ribosomal proteins methylation.•The protein lysine methyltransferase, SET7/9 interacts with the large ribosomal protein eL42.•SET7/9 methylates eL42 at three different lysine residues both in vitro and in vivo.•SET7/9 mediated methylation of eL42 affects the global translation. |
| doi_str_mv | 10.1016/j.bbamcr.2019.118611 |
| format | Article |
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[Display omitted]
•Little is known about the regulation and functional significance of ribosomal proteins methylation.•The protein lysine methyltransferase, SET7/9 interacts with the large ribosomal protein eL42.•SET7/9 methylates eL42 at three different lysine residues both in vitro and in vivo.•SET7/9 mediated methylation of eL42 affects the global translation.</description><identifier>ISSN: 0167-4889</identifier><identifier>EISSN: 1879-2596</identifier><identifier>DOI: 10.1016/j.bbamcr.2019.118611</identifier><identifier>PMID: 31751593</identifier><language>eng</language><publisher>AMSTERDAM: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Biochemistry & Molecular Biology ; Cell Biology ; HEK293 Cells ; Histone-Lysine N-Methyltransferase - antagonists & inhibitors ; Histone-Lysine N-Methyltransferase - genetics ; Histone-Lysine N-Methyltransferase - metabolism ; Humans ; Life Sciences & Biomedicine ; Lysine - chemistry ; Lysine methylation ; Methylation ; Protein Biosynthesis ; Protein Domains ; Protein Interaction Domains and Motifs ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Protein-protein interaction ; Ribosomal Proteins - chemistry ; Ribosomal Proteins - genetics ; Ribosomal Proteins - metabolism ; RNA Interference ; RNA, Small Interfering - metabolism ; RPL36A ; Science & Technology ; SETD7 ; Translation ; Two-Hybrid System Techniques</subject><ispartof>Biochimica et biophysica acta. Molecular cell research, 2020-02, Vol.1867 (2), p.118611, Article 118611</ispartof><rights>2019 Elsevier B.V.</rights><rights>Copyright © 2019 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>8</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000508740900009</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c408t-8e1fccf77a1f0e2f7dbddb1248cfc1ed2a1c4fb267e1826474767f5264dbd3d93</citedby><cites>FETCH-LOGICAL-c408t-8e1fccf77a1f0e2f7dbddb1248cfc1ed2a1c4fb267e1826474767f5264dbd3d93</cites><orcidid>0000-0001-6666-8925 ; 0000-0003-2588-9865 ; 0000-0002-0943-0264 ; 0000-0002-4980-8014</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbamcr.2019.118611$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,28253,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31751593$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mahesh, Arun</creatorcontrib><creatorcontrib>Khan, Mohd. Imran K.</creatorcontrib><creatorcontrib>Govindaraju, Gayathri</creatorcontrib><creatorcontrib>Verma, Mamta</creatorcontrib><creatorcontrib>Awasthi, Sharad</creatorcontrib><creatorcontrib>Chavali, Pavithra L.</creatorcontrib><creatorcontrib>Chavali, Sreenivas</creatorcontrib><creatorcontrib>Rajavelu, Arumugam</creatorcontrib><creatorcontrib>Dhayalan, Arunkumar</creatorcontrib><title>SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis</title><title>Biochimica et biophysica acta. Molecular cell research</title><addtitle>BBA-MOL CELL RES</addtitle><addtitle>Biochim Biophys Acta Mol Cell Res</addtitle><description>Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9-mediated methylation often regulates the stability, sub-cellular localization and protein-protein interactions of its substrate proteins. Here, we aimed to identify novel biological processes regulated by SET7/9 by identifying new interaction partners. For this we used yeast two-hybrid screening and identified the large subunit ribosomal protein, eL42 as a potential interactor of SET7/9. We confirmed the SET7/9-eL42 interaction by co-immunoprecipitation and GST pulldown studies. The N-terminal MORN domain of SET7/9 is essential for its interaction with eL42. Importantly, we identified that SET7/9 methylates eL42 at three different lysines - Lys53, Lys80 and Lys100 through site-directed mutagenesis. By puromycin incorporation assay, we find that SET7/9-mediated methylation of eL42 affects global translation. This study identifies a new role of the functionally versatile SET7/9 lysine methyltransferase in the regulation of global protein synthesis.
[Display omitted]
•Little is known about the regulation and functional significance of ribosomal proteins methylation.•The protein lysine methyltransferase, SET7/9 interacts with the large ribosomal protein eL42.•SET7/9 methylates eL42 at three different lysine residues both in vitro and in vivo.•SET7/9 mediated methylation of eL42 affects the global translation.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry & Molecular Biology</subject><subject>Cell Biology</subject><subject>HEK293 Cells</subject><subject>Histone-Lysine N-Methyltransferase - antagonists & inhibitors</subject><subject>Histone-Lysine N-Methyltransferase - genetics</subject><subject>Histone-Lysine N-Methyltransferase - metabolism</subject><subject>Humans</subject><subject>Life Sciences & Biomedicine</subject><subject>Lysine - chemistry</subject><subject>Lysine methylation</subject><subject>Methylation</subject><subject>Protein Biosynthesis</subject><subject>Protein Domains</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>Protein-protein interaction</subject><subject>Ribosomal Proteins - chemistry</subject><subject>Ribosomal Proteins - genetics</subject><subject>Ribosomal Proteins - metabolism</subject><subject>RNA Interference</subject><subject>RNA, Small Interfering - metabolism</subject><subject>RPL36A</subject><subject>Science & Technology</subject><subject>SETD7</subject><subject>Translation</subject><subject>Two-Hybrid System Techniques</subject><issn>0167-4889</issn><issn>1879-2596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><recordid>eNqNkM9r2zAUgEVZabO0_8EYvm9O9RzZki6DYbIfEOih7akHIUtPrUJsB0npyH8_ZU57HNVFAn3fg_cR8gnoAig0N5tF1-nehEVFQS4ARANwRmYguCyrWjYfyCxjvGRCyEvyMcYNzYfx-oJcLoHXUMvljDzere75jSz8kDBok2KhB1v0mJ4PW50wFukZi-C7MY693ha7MCb0w9cC16z6hwZ82k_k6a-IhyFL0ccrcu70NuL16Z6Thx-r-_ZXub79-bv9vi4NoyKVAsEZ4zjX4ChWjtvO2g4qJowzgLbSYJjrqoYjiKphnPGGuzq_Mri0cjknbJprwhhjQKd2wfc6HBRQdWylNmpqpY6t1NQqa58nbbfverRv0mucDIgJ-IPd6KLxOBh8w3LMmgrOqDx2la1POvlxaMf9kLL65f1qpr9NNOZKLx6DOhnWBzRJ2dH_f5W_j5KeFg</recordid><startdate>202002</startdate><enddate>202002</enddate><creator>Mahesh, Arun</creator><creator>Khan, Mohd. 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Imran K.</creatorcontrib><creatorcontrib>Govindaraju, Gayathri</creatorcontrib><creatorcontrib>Verma, Mamta</creatorcontrib><creatorcontrib>Awasthi, Sharad</creatorcontrib><creatorcontrib>Chavali, Pavithra L.</creatorcontrib><creatorcontrib>Chavali, Sreenivas</creatorcontrib><creatorcontrib>Rajavelu, Arumugam</creatorcontrib><creatorcontrib>Dhayalan, Arunkumar</creatorcontrib><collection>Web of Science - Science Citation Index Expanded - 2020</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochimica et biophysica acta. Molecular cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mahesh, Arun</au><au>Khan, Mohd. Imran K.</au><au>Govindaraju, Gayathri</au><au>Verma, Mamta</au><au>Awasthi, Sharad</au><au>Chavali, Pavithra L.</au><au>Chavali, Sreenivas</au><au>Rajavelu, Arumugam</au><au>Dhayalan, Arunkumar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis</atitle><jtitle>Biochimica et biophysica acta. Molecular cell research</jtitle><stitle>BBA-MOL CELL RES</stitle><addtitle>Biochim Biophys Acta Mol Cell Res</addtitle><date>2020-02</date><risdate>2020</risdate><volume>1867</volume><issue>2</issue><spage>118611</spage><pages>118611-</pages><artnum>118611</artnum><issn>0167-4889</issn><eissn>1879-2596</eissn><abstract>Methylation of proteins is emerging to be an important regulator of protein function. SET7/9, a protein lysine methyltransferase, catalyses methylation of several proteins involved in diverse biological processes. SET7/9-mediated methylation often regulates the stability, sub-cellular localization and protein-protein interactions of its substrate proteins. Here, we aimed to identify novel biological processes regulated by SET7/9 by identifying new interaction partners. For this we used yeast two-hybrid screening and identified the large subunit ribosomal protein, eL42 as a potential interactor of SET7/9. We confirmed the SET7/9-eL42 interaction by co-immunoprecipitation and GST pulldown studies. The N-terminal MORN domain of SET7/9 is essential for its interaction with eL42. Importantly, we identified that SET7/9 methylates eL42 at three different lysines - Lys53, Lys80 and Lys100 through site-directed mutagenesis. By puromycin incorporation assay, we find that SET7/9-mediated methylation of eL42 affects global translation. This study identifies a new role of the functionally versatile SET7/9 lysine methyltransferase in the regulation of global protein synthesis.
[Display omitted]
•Little is known about the regulation and functional significance of ribosomal proteins methylation.•The protein lysine methyltransferase, SET7/9 interacts with the large ribosomal protein eL42.•SET7/9 methylates eL42 at three different lysine residues both in vitro and in vivo.•SET7/9 mediated methylation of eL42 affects the global translation.</abstract><cop>AMSTERDAM</cop><pub>Elsevier B.V</pub><pmid>31751593</pmid><doi>10.1016/j.bbamcr.2019.118611</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-6666-8925</orcidid><orcidid>https://orcid.org/0000-0003-2588-9865</orcidid><orcidid>https://orcid.org/0000-0002-0943-0264</orcidid><orcidid>https://orcid.org/0000-0002-4980-8014</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present); Web of Science - Science Citation Index Expanded - 2020<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" /> |
| subjects | Amino Acid Sequence Biochemistry & Molecular Biology Cell Biology HEK293 Cells Histone-Lysine N-Methyltransferase - antagonists & inhibitors Histone-Lysine N-Methyltransferase - genetics Histone-Lysine N-Methyltransferase - metabolism Humans Life Sciences & Biomedicine Lysine - chemistry Lysine methylation Methylation Protein Biosynthesis Protein Domains Protein Interaction Domains and Motifs Protein Subunits - chemistry Protein Subunits - metabolism Protein-protein interaction Ribosomal Proteins - chemistry Ribosomal Proteins - genetics Ribosomal Proteins - metabolism RNA Interference RNA, Small Interfering - metabolism RPL36A Science & Technology SETD7 Translation Two-Hybrid System Techniques |
| title | SET7/9 interacts and methylates the ribosomal protein, eL42 and regulates protein synthesis |
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