Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation
RNA tails play integral roles in the regulation of messenger RNA (mRNA) translation and decay. Guanylation of the poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TENT4A (PAPD7) and TENT4B (PAPD5) as the enzymes responsible for mRNA guanylation....
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2018-08, Vol.361 (6403), p.701-704 |
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| creator | Lim, Jaechul Kim, Dongwan Lee, Young-Suk Ha, Minju Lee, Mihye Yeo, Jinah Chang, Hyeshik Song, Jaewon Ahn, Kwangseog Kim, V Narry |
| description | RNA tails play integral roles in the regulation of messenger RNA (mRNA) translation and decay. Guanylation of the poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TENT4A (PAPD7) and TENT4B (PAPD5) as the enzymes responsible for mRNA guanylation. Purified TENT4 proteins generate a mixed poly(A) tail with intermittent non-adenosine residues, the most common of which is guanosine. A single guanosine residue is sufficient to impede the deadenylase CCR4-NOT complex, which trims the tail and exposes guanosine at the 3' end. Consistently, depletion of TENT4A and TENT4B leads to a decrease in mRNA half-life and abundance in cells. Thus, TENT4A and TENT4B produce a mixed tail that shields mRNA from rapid deadenylation. Our study unveils the role of mixed tailing and expands the complexity of posttranscriptional gene regulation. |
| doi_str_mv | 10.1126/science.aam5794 |
| format | Article |
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Guanylation of the poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TENT4A (PAPD7) and TENT4B (PAPD5) as the enzymes responsible for mRNA guanylation. Purified TENT4 proteins generate a mixed poly(A) tail with intermittent non-adenosine residues, the most common of which is guanosine. A single guanosine residue is sufficient to impede the deadenylase CCR4-NOT complex, which trims the tail and exposes guanosine at the 3' end. Consistently, depletion of TENT4A and TENT4B leads to a decrease in mRNA half-life and abundance in cells. Thus, TENT4A and TENT4B produce a mixed tail that shields mRNA from rapid deadenylation. Our study unveils the role of mixed tailing and expands the complexity of posttranscriptional gene regulation.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aam5794</identifier><identifier>PMID: 30026317</identifier><language>eng</language><publisher>United States: The American Association for the Advancement of Science</publisher><subject>Adenosine ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Complexity ; DNA-Directed DNA Polymerase - genetics ; DNA-Directed DNA Polymerase - metabolism ; Enzymes ; Enzymology ; Exoribonucleases - metabolism ; Fibroblasts ; Gene Deletion ; Gene expression ; Gene Expression Regulation ; Gene Knockout Techniques ; Gene regulation ; Guanosine ; HEK293 Cells ; HeLa Cells ; Humans ; mRNA ; mRNA stability ; mRNA turnover ; Nucleotides ; Polyadenine ; Polyadenylation ; Post-transcription ; Proteins ; Residues ; Ribonucleic acid ; RNA ; RNA 3' End Processing ; RNA Nucleotidyltransferases - genetics ; RNA Nucleotidyltransferases - metabolism ; RNA, Messenger - metabolism ; Shields</subject><ispartof>Science (American Association for the Advancement of Science), 2018-08, Vol.361 (6403), p.701-704</ispartof><rights>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</rights><rights>Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c469t-af3bb333cb2da8a2f660bced3975ad313e55f12ff34c0ef97f3d8a7d2e7fb1c33</citedby><cites>FETCH-LOGICAL-c469t-af3bb333cb2da8a2f660bced3975ad313e55f12ff34c0ef97f3d8a7d2e7fb1c33</cites><orcidid>0000-0002-9387-1942 ; 0000-0003-0220-9951 ; 0000-0002-3213-4965 ; 0000-0003-2328-415X ; 0000-0003-2251-3707 ; 0000-0002-6075-2656 ; 0000-0002-9812-8015</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,2871,2872,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30026317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lim, Jaechul</creatorcontrib><creatorcontrib>Kim, Dongwan</creatorcontrib><creatorcontrib>Lee, Young-Suk</creatorcontrib><creatorcontrib>Ha, Minju</creatorcontrib><creatorcontrib>Lee, Mihye</creatorcontrib><creatorcontrib>Yeo, Jinah</creatorcontrib><creatorcontrib>Chang, Hyeshik</creatorcontrib><creatorcontrib>Song, Jaewon</creatorcontrib><creatorcontrib>Ahn, Kwangseog</creatorcontrib><creatorcontrib>Kim, V Narry</creatorcontrib><title>Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>RNA tails play integral roles in the regulation of messenger RNA (mRNA) translation and decay. Guanylation of the poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TENT4A (PAPD7) and TENT4B (PAPD5) as the enzymes responsible for mRNA guanylation. Purified TENT4 proteins generate a mixed poly(A) tail with intermittent non-adenosine residues, the most common of which is guanosine. A single guanosine residue is sufficient to impede the deadenylase CCR4-NOT complex, which trims the tail and exposes guanosine at the 3' end. Consistently, depletion of TENT4A and TENT4B leads to a decrease in mRNA half-life and abundance in cells. Thus, TENT4A and TENT4B produce a mixed tail that shields mRNA from rapid deadenylation. Our study unveils the role of mixed tailing and expands the complexity of posttranscriptional gene regulation.</description><subject>Adenosine</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Complexity</subject><subject>DNA-Directed DNA Polymerase - genetics</subject><subject>DNA-Directed DNA Polymerase - metabolism</subject><subject>Enzymes</subject><subject>Enzymology</subject><subject>Exoribonucleases - metabolism</subject><subject>Fibroblasts</subject><subject>Gene Deletion</subject><subject>Gene expression</subject><subject>Gene Expression Regulation</subject><subject>Gene Knockout Techniques</subject><subject>Gene regulation</subject><subject>Guanosine</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>mRNA</subject><subject>mRNA stability</subject><subject>mRNA turnover</subject><subject>Nucleotides</subject><subject>Polyadenine</subject><subject>Polyadenylation</subject><subject>Post-transcription</subject><subject>Proteins</subject><subject>Residues</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA 3' End Processing</subject><subject>RNA Nucleotidyltransferases - genetics</subject><subject>RNA Nucleotidyltransferases - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Shields</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LAzEQhoMotlbP3iTgedsks9ndHGupVqgVpJ6XfGrKftRkC_bfu9JV5jAD884z8CB0S8mUUpbNova20XYqZc1zkZ6hMSWCJ4IROEdjQiBLCpLzEbqKcUdIvxNwiUZACMuA5mO0evHf1uBO-so3H1gd8Xa52aZzLBtzGh9w_PS2MhHXb5s5dqGtcZB7b7Cx0tjmWMnOt801unCyivZm6BP0_rjcLlbJ-vXpeTFfJzrNRJdIB0oBgFbMyEIyl2VEaWtA5FwaoGA5d5Q5B6km1oncgSlkbpjNnaIaYILuT9x9aL8ONnblrj2Epn9ZMlKInsD7mqDZKaVDG2OwrtwHX8twLCkpf82Vg7lyMNdf3A3cg6qt-c__qYIf2cBq0w</recordid><startdate>20180817</startdate><enddate>20180817</enddate><creator>Lim, Jaechul</creator><creator>Kim, Dongwan</creator><creator>Lee, Young-Suk</creator><creator>Ha, Minju</creator><creator>Lee, Mihye</creator><creator>Yeo, Jinah</creator><creator>Chang, Hyeshik</creator><creator>Song, Jaewon</creator><creator>Ahn, Kwangseog</creator><creator>Kim, V Narry</creator><general>The American Association for the Advancement of Science</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><orcidid>https://orcid.org/0000-0002-9387-1942</orcidid><orcidid>https://orcid.org/0000-0003-0220-9951</orcidid><orcidid>https://orcid.org/0000-0002-3213-4965</orcidid><orcidid>https://orcid.org/0000-0003-2328-415X</orcidid><orcidid>https://orcid.org/0000-0003-2251-3707</orcidid><orcidid>https://orcid.org/0000-0002-6075-2656</orcidid><orcidid>https://orcid.org/0000-0002-9812-8015</orcidid></search><sort><creationdate>20180817</creationdate><title>Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation</title><author>Lim, Jaechul ; Kim, Dongwan ; Lee, Young-Suk ; Ha, Minju ; Lee, Mihye ; Yeo, Jinah ; Chang, Hyeshik ; Song, Jaewon ; Ahn, Kwangseog ; Kim, V Narry</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c469t-af3bb333cb2da8a2f660bced3975ad313e55f12ff34c0ef97f3d8a7d2e7fb1c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adenosine</topic><topic>Chromosomal Proteins, Non-Histone - genetics</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>Complexity</topic><topic>DNA-Directed DNA Polymerase - genetics</topic><topic>DNA-Directed DNA Polymerase - metabolism</topic><topic>Enzymes</topic><topic>Enzymology</topic><topic>Exoribonucleases - metabolism</topic><topic>Fibroblasts</topic><topic>Gene Deletion</topic><topic>Gene expression</topic><topic>Gene Expression Regulation</topic><topic>Gene Knockout Techniques</topic><topic>Gene regulation</topic><topic>Guanosine</topic><topic>HEK293 Cells</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>mRNA</topic><topic>mRNA stability</topic><topic>mRNA turnover</topic><topic>Nucleotides</topic><topic>Polyadenine</topic><topic>Polyadenylation</topic><topic>Post-transcription</topic><topic>Proteins</topic><topic>Residues</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA 3' End Processing</topic><topic>RNA Nucleotidyltransferases - genetics</topic><topic>RNA Nucleotidyltransferases - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>Shields</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lim, Jaechul</creatorcontrib><creatorcontrib>Kim, Dongwan</creatorcontrib><creatorcontrib>Lee, Young-Suk</creatorcontrib><creatorcontrib>Ha, Minju</creatorcontrib><creatorcontrib>Lee, Mihye</creatorcontrib><creatorcontrib>Yeo, Jinah</creatorcontrib><creatorcontrib>Chang, Hyeshik</creatorcontrib><creatorcontrib>Song, Jaewon</creatorcontrib><creatorcontrib>Ahn, Kwangseog</creatorcontrib><creatorcontrib>Kim, V Narry</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lim, Jaechul</au><au>Kim, Dongwan</au><au>Lee, Young-Suk</au><au>Ha, Minju</au><au>Lee, Mihye</au><au>Yeo, Jinah</au><au>Chang, Hyeshik</au><au>Song, Jaewon</au><au>Ahn, Kwangseog</au><au>Kim, V Narry</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2018-08-17</date><risdate>2018</risdate><volume>361</volume><issue>6403</issue><spage>701</spage><epage>704</epage><pages>701-704</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>RNA tails play integral roles in the regulation of messenger RNA (mRNA) translation and decay. Guanylation of the poly(A) tail was discovered recently, yet the enzymology and function remain obscure. Here we identify TENT4A (PAPD7) and TENT4B (PAPD5) as the enzymes responsible for mRNA guanylation. Purified TENT4 proteins generate a mixed poly(A) tail with intermittent non-adenosine residues, the most common of which is guanosine. A single guanosine residue is sufficient to impede the deadenylase CCR4-NOT complex, which trims the tail and exposes guanosine at the 3' end. Consistently, depletion of TENT4A and TENT4B leads to a decrease in mRNA half-life and abundance in cells. Thus, TENT4A and TENT4B produce a mixed tail that shields mRNA from rapid deadenylation. Our study unveils the role of mixed tailing and expands the complexity of posttranscriptional gene regulation.</abstract><cop>United States</cop><pub>The American Association for the Advancement of Science</pub><pmid>30026317</pmid><doi>10.1126/science.aam5794</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-9387-1942</orcidid><orcidid>https://orcid.org/0000-0003-0220-9951</orcidid><orcidid>https://orcid.org/0000-0002-3213-4965</orcidid><orcidid>https://orcid.org/0000-0003-2328-415X</orcidid><orcidid>https://orcid.org/0000-0003-2251-3707</orcidid><orcidid>https://orcid.org/0000-0002-6075-2656</orcidid><orcidid>https://orcid.org/0000-0002-9812-8015</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Chromosomal Proteins, Non-Histone - genetics Chromosomal Proteins, Non-Histone - metabolism Complexity DNA-Directed DNA Polymerase - genetics DNA-Directed DNA Polymerase - metabolism Enzymes Enzymology Exoribonucleases - metabolism Fibroblasts Gene Deletion Gene expression Gene Expression Regulation Gene Knockout Techniques Gene regulation Guanosine HEK293 Cells HeLa Cells Humans mRNA mRNA stability mRNA turnover Nucleotides Polyadenine Polyadenylation Post-transcription Proteins Residues Ribonucleic acid RNA RNA 3' End Processing RNA Nucleotidyltransferases - genetics RNA Nucleotidyltransferases - metabolism RNA, Messenger - metabolism Shields |
| title | Mixed tailing by TENT4A and TENT4B shields mRNA from rapid deadenylation |
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