Hypermethylated-capped selenoprotein mRNAs in mammals

Mammalian mRNAs are generated by complex and coordinated biogenesis pathways and acquire 5'-end m(7)G caps that play fundamental roles in processing and translation. Here we show that several selenoprotein mRNAs are not recognized efficiently by translation initiation factor eIF4E because they...

Full description

Saved in:
Bibliographic Details
Published inNucleic acids research Vol. 42; no. 13; pp. 8663 - 8677
Main Authors Wurth, Laurence, Gribling-Burrer, Anne-Sophie, Verheggen, Céline, Leichter, Michael, Takeuchi, Akiko, Baudrey, Stéphanie, Martin, Franck, Krol, Alain, Bertrand, Edouard, Allmang, Christine
Format Journal Article
LanguageEnglish
Published England Oxford University Press 29.07.2014
Subjects
Cell Line
Eukaryotic Initiation Factor-4E - metabolism
Glutathione Peroxidase - biosynthesis
Glutathione Peroxidase - genetics
Humans
Methylation
Methyltransferases - metabolism
Nuclear Proteins - metabolism
Polyribosomes - chemistry
Protein Biosynthesis
Ribonucleoproteins, Small Nucleolar - metabolism
RNA
RNA Caps - metabolism
RNA, Messenger - analysis
RNA, Messenger - metabolism
RNA-Binding Proteins - metabolism
Selenoproteins - biosynthesis
Selenoproteins - genetics
Selenoproteins - metabolism
SMN Complex Proteins - metabolism
Online AccessGet full text

Cover

More Information
Summary:Mammalian mRNAs are generated by complex and coordinated biogenesis pathways and acquire 5'-end m(7)G caps that play fundamental roles in processing and translation. Here we show that several selenoprotein mRNAs are not recognized efficiently by translation initiation factor eIF4E because they bear a hypermethylated cap. This cap modification is acquired via a 5'-end maturation pathway similar to that of the small nucle(ol)ar RNAs (sn- and snoRNAs). Our findings also establish that the trimethylguanosine synthase 1 (Tgs1) interacts with selenoprotein mRNAs for cap hypermethylation and that assembly chaperones and core proteins devoted to sn- and snoRNP maturation contribute to recruiting Tgs1 to selenoprotein mRNPs. We further demonstrate that the hypermethylated-capped selenoprotein mRNAs localize to the cytoplasm, are associated with polysomes and thus translated. Moreover, we found that the activity of Tgs1, but not of eIF4E, is required for the synthesis of the GPx1 selenoprotein in vivo.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gku580