Translational Stability of Native and Deadenylylated Rabbit Globin mRNA Injected into HeLa Cells
HeLa human cells were injected with a natural mixture of rabbit α and β globin mRNA. They were incubated for 6 hr with [35S]methionine either immediately after injection or 20 hr later. The labeled proteins in the injected cells were analyzed by fluorography of two-dimensional electrophoresis gels....
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1981-02, Vol.78 (2), p.908-911 |
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creator | Huez, Georges Bruck, Claudine Cleuter, Yvette |
description | HeLa human cells were injected with a natural mixture of rabbit α and β globin mRNA. They were incubated for 6 hr with [35S]methionine either immediately after injection or 20 hr later. The labeled proteins in the injected cells were analyzed by fluorography of two-dimensional electrophoresis gels. By using this procedure, it was possible to show that, during the first few hours after injection, both α and β globin molecules are synthesized with an α to β ratio approximately equal to 0.6. The rate of synthesis of α globin decreased significantly faster than that of β globin over a 26-hr period after injection of the two mRNAs. It thus seems that two messenger RNAs coding for closely related polypeptides possess a markedly different translational stability. When deadenylylated rabbit globin mRNAs were injected into HeLa cells, no globin synthesis could be detected by the techniques used. We conclude that the translational half-life of mRNAs lacking poly(A) is very short in these cells. It is thus clear that the poly(A) segment is required to ensure stability to globin mRNA in somatic cells as in Xenopus oocytes. |
doi_str_mv | 10.1073/pnas.78.2.908 |
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They were incubated for 6 hr with [35S]methionine either immediately after injection or 20 hr later. The labeled proteins in the injected cells were analyzed by fluorography of two-dimensional electrophoresis gels. By using this procedure, it was possible to show that, during the first few hours after injection, both α and β globin molecules are synthesized with an α to β ratio approximately equal to 0.6. The rate of synthesis of α globin decreased significantly faster than that of β globin over a 26-hr period after injection of the two mRNAs. It thus seems that two messenger RNAs coding for closely related polypeptides possess a markedly different translational stability. When deadenylylated rabbit globin mRNAs were injected into HeLa cells, no globin synthesis could be detected by the techniques used. We conclude that the translational half-life of mRNAs lacking poly(A) is very short in these cells. It is thus clear that the poly(A) segment is required to ensure stability to globin mRNA in somatic cells as in Xenopus oocytes.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.78.2.908</identifier><identifier>PMID: 6940155</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenine ; Animals ; Biochemistry ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Female ; Gels ; Globins - genetics ; Half lives ; HeLa cells ; HeLa Cells - metabolism ; Humans ; Messenger RNA ; Methionine - metabolism ; Molecules ; Oocytes ; Oocytes - metabolism ; Protein Biosynthesis ; Rabbits ; RNA ; RNA, Messenger - genetics ; Somatic cells ; Xenopus</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1981-02, Vol.78 (2), p.908-911</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3668-605f6dd8f5f2fa2be0372e868d0bb6b302cdbd32d017cfc868fd059a8e6897d33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/78/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/10314$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/10314$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6940155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huez, Georges</creatorcontrib><creatorcontrib>Bruck, Claudine</creatorcontrib><creatorcontrib>Cleuter, Yvette</creatorcontrib><title>Translational Stability of Native and Deadenylylated Rabbit Globin mRNA Injected into HeLa Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>HeLa human cells were injected with a natural mixture of rabbit α and β globin mRNA. They were incubated for 6 hr with [35S]methionine either immediately after injection or 20 hr later. The labeled proteins in the injected cells were analyzed by fluorography of two-dimensional electrophoresis gels. By using this procedure, it was possible to show that, during the first few hours after injection, both α and β globin molecules are synthesized with an α to β ratio approximately equal to 0.6. The rate of synthesis of α globin decreased significantly faster than that of β globin over a 26-hr period after injection of the two mRNAs. It thus seems that two messenger RNAs coding for closely related polypeptides possess a markedly different translational stability. When deadenylylated rabbit globin mRNAs were injected into HeLa cells, no globin synthesis could be detected by the techniques used. We conclude that the translational half-life of mRNAs lacking poly(A) is very short in these cells. It is thus clear that the poly(A) segment is required to ensure stability to globin mRNA in somatic cells as in Xenopus oocytes.</description><subject>Adenine</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Gels</subject><subject>Globins - genetics</subject><subject>Half lives</subject><subject>HeLa cells</subject><subject>HeLa Cells - metabolism</subject><subject>Humans</subject><subject>Messenger RNA</subject><subject>Methionine - metabolism</subject><subject>Molecules</subject><subject>Oocytes</subject><subject>Oocytes - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Rabbits</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>Somatic cells</subject><subject>Xenopus</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUFvFCEYhomxqWv16MVowkVvs34MMwxz8NBstW2yqUmtZ4QBlA0L68A23X8vk90268UTCc_z8n3kRegNgTmBjn7aBJnmHZ_X8x74MzQj0JOKNT08RzOAuqt4Uzcv0MuUVgDQtxxO0SnrGyBtO0M_70YZkpfZxSA9_p6lct7lHY4W35Tbe4Nl0PjCSG3Czu-KaTS-lUq5jC99VC7g9e3NOb4OKzNMzIUc8ZVZSrww3qdX6MRKn8zrw3mGfnz9cre4qpbfLq8X58tqoIzxikFrmdbctra2slYGaFcbzrgGpZiiUA9aaVprIN1ghwKshraX3DDed5rSM_R5_-5mq9ZGDybkUXqxGd1ajjsRpRP_kuB-i1_xXlDS92TKfzzkx_hna1IWa5eG8gMZTNwm0bWsacuoIlZ7cRhjSqOxTzMIiKkRMTUiOi5qURop_vvjxZ7sQwWFvzvwKfZIj-If_oOF3XqfzUMu3tu9t0o5jkc7UdLQvyHiqSM</recordid><startdate>19810201</startdate><enddate>19810201</enddate><creator>Huez, Georges</creator><creator>Bruck, Claudine</creator><creator>Cleuter, Yvette</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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></search><sort><creationdate>19810201</creationdate><title>Translational Stability of Native and Deadenylylated Rabbit Globin mRNA Injected into HeLa Cells</title><author>Huez, Georges ; Bruck, Claudine ; Cleuter, Yvette</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3668-605f6dd8f5f2fa2be0372e868d0bb6b302cdbd32d017cfc868fd059a8e6897d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adenine</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Electrophoresis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Gels</topic><topic>Globins - genetics</topic><topic>Half lives</topic><topic>HeLa cells</topic><topic>HeLa Cells - metabolism</topic><topic>Humans</topic><topic>Messenger RNA</topic><topic>Methionine - metabolism</topic><topic>Molecules</topic><topic>Oocytes</topic><topic>Oocytes - metabolism</topic><topic>Protein Biosynthesis</topic><topic>Rabbits</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><topic>Somatic cells</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huez, Georges</creatorcontrib><creatorcontrib>Bruck, Claudine</creatorcontrib><creatorcontrib>Cleuter, Yvette</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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huez, Georges</au><au>Bruck, Claudine</au><au>Cleuter, Yvette</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Translational Stability of Native and Deadenylylated Rabbit Globin mRNA Injected into HeLa Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1981-02-01</date><risdate>1981</risdate><volume>78</volume><issue>2</issue><spage>908</spage><epage>911</epage><pages>908-911</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>HeLa human cells were injected with a natural mixture of rabbit α and β globin mRNA. They were incubated for 6 hr with [35S]methionine either immediately after injection or 20 hr later. The labeled proteins in the injected cells were analyzed by fluorography of two-dimensional electrophoresis gels. By using this procedure, it was possible to show that, during the first few hours after injection, both α and β globin molecules are synthesized with an α to β ratio approximately equal to 0.6. The rate of synthesis of α globin decreased significantly faster than that of β globin over a 26-hr period after injection of the two mRNAs. It thus seems that two messenger RNAs coding for closely related polypeptides possess a markedly different translational stability. When deadenylylated rabbit globin mRNAs were injected into HeLa cells, no globin synthesis could be detected by the techniques used. We conclude that the translational half-life of mRNAs lacking poly(A) is very short in these cells. It is thus clear that the poly(A) segment is required to ensure stability to globin mRNA in somatic cells as in Xenopus oocytes.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6940155</pmid><doi>10.1073/pnas.78.2.908</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenine Animals Biochemistry Electrophoresis Electrophoresis, Polyacrylamide Gel Female Gels Globins - genetics Half lives HeLa cells HeLa Cells - metabolism Humans Messenger RNA Methionine - metabolism Molecules Oocytes Oocytes - metabolism Protein Biosynthesis Rabbits RNA RNA, Messenger - genetics Somatic cells Xenopus |
title | Translational Stability of Native and Deadenylylated Rabbit Globin mRNA Injected into HeLa Cells |
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