2′,3′‐Cyclic nucleotide 3′‐phosphodiesterase: A novel RNA‐binding protein that inhibits protein synthesis
Identifieur interne : 002925 ( Main/Exploration ); précédent : 002924; suivant : 0029262′,3′‐Cyclic nucleotide 3′‐phosphodiesterase: A novel RNA‐binding protein that inhibits protein synthesis
Auteurs : Michel Gravel [Canada] ; Francis Robert [Canada] ; Vicky Kottis [Canada] ; Imed-Eddine Gallouzi [Canada] ; Jerry Pelletier [Canada] ; Peter E. Braun [Canada]Source :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2009-04.
English descriptors
- Teeft :
- Agarose, Agarose beads, Agrawal, Amino acids, Aptamers, Assay, Autoradiography, Biol, Biol chem, Braun, Catalytic, Catalytic domain, Chem, Cnp1, Cnp2, Cnpase, Cnpase activity, Contract grant sponsor, Cyclic, Cyclic nucleotide, Cyclic phosphodiesterase, Cytoplasmic, Enzymatic activity, Evdokimova, Ffluc, Ffluc mrna, Inhibitory effect, Kozlov, Ligase, Luciferase, Luciferase activity, Mcgill university, Mrna, Myelin, Neuroscience, Neuroscience research, Novel protein, Nucleic, Nucleic acids, Nucleotide, Nylon membrane, Odcs, Optic nerve regeneration, Ovchinnikov, Phosphodiesterase, Phosphorylation, Proc natl acad, Promega, Protein synthesis, Reticulocyte, Ribosome, Selex, Translation inhibition, Trna, Tubulin, Wheat germ.
Abstract
2′,3′‐Cyclic nucleotide 3′‐phosphodiesterase (CNP) is one of the earliest myelin‐related proteins to be specifically expressed in differentiating oligodendrocytes (ODCs) in the central nervous system (CNS) and is implicated in myelin biogenesis. CNP possesses an in vitro enzymatic activity, whose in vivo relevance remains to be defined, because substrates with 2′,3,‐cyclic termini have not yet been identified. To characterize CNP function better, we previously determined the structure of the CNP catalytic domain by NMR. Interestingly, the structure is remarkably similar to the plant cyclic nucleotide phosphodiesterase (CPDase) from A. thaliana and the bacterial 2′‐5′ RNA ligase from T. thermophilus, which are known to play roles in RNA metabolism. Here we show that CNP is an RNA‐binding protein. Furthermore, by using precipitation analyses, we demonstrate that CNP associates with poly(A)+ mRNAs in vivo and suppresses translation in vitro in a dose‐dependent manner. With SELEX, we isolated RNA aptamers that can suppress the inhibitory effect of CNP on translation. We also demonstrate that CNP1 can bridge an association between tubulin and RNA. These results suggest that CNP1 may regulate expression of mRNAs in ODCs of the CNS. © 2008 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jnr.21939
Affiliations:
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CNP possesses an in vitro enzymatic activity, whose in vivo relevance remains to be defined, because substrates with 2′,3,‐cyclic termini have not yet been identified. To characterize CNP function better, we previously determined the structure of the CNP catalytic domain by NMR. Interestingly, the structure is remarkably similar to the plant cyclic nucleotide phosphodiesterase (CPDase) from A. thaliana and the bacterial 2′‐5′ RNA ligase from T. thermophilus, which are known to play roles in RNA metabolism. Here we show that CNP is an RNA‐binding protein. Furthermore, by using precipitation analyses, we demonstrate that CNP associates with poly(A)+ mRNAs in vivo and suppresses translation in vitro in a dose‐dependent manner. With SELEX, we isolated RNA aptamers that can suppress the inhibitory effect of CNP on translation. We also demonstrate that CNP1 can bridge an association between tubulin and RNA. These results suggest that CNP1 may regulate expression of mRNAs in ODCs of the CNS. © 2008 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>Canada</li></country><region><li>Québec</li></region><settlement><li>Montréal</li></settlement><orgName><li>Université McGill</li></orgName></list><tree><country name="Canada"><region name="Québec"><name sortKey="Gravel, Michel" sort="Gravel, Michel" uniqKey="Gravel M" first="Michel" last="Gravel">Michel Gravel</name></region><name sortKey="Braun, Peter E" sort="Braun, Peter E" uniqKey="Braun P" first="Peter E." last="Braun">Peter E. Braun</name><name sortKey="Gallouzi, Imed Ddine" sort="Gallouzi, Imed Ddine" uniqKey="Gallouzi I" first="Imed-Eddine" last="Gallouzi">Imed-Eddine Gallouzi</name><name sortKey="Kottis, Vicky" sort="Kottis, Vicky" uniqKey="Kottis V" first="Vicky" last="Kottis">Vicky Kottis</name><name sortKey="Pelletier, Jerry" sort="Pelletier, Jerry" uniqKey="Pelletier J" first="Jerry" last="Pelletier">Jerry Pelletier</name><name sortKey="Pelletier, Jerry" sort="Pelletier, Jerry" uniqKey="Pelletier J" first="Jerry" last="Pelletier">Jerry Pelletier</name><name sortKey="Pelletier, Jerry" sort="Pelletier, Jerry" uniqKey="Pelletier J" first="Jerry" last="Pelletier">Jerry Pelletier</name><name sortKey="Pelletier, Jerry" sort="Pelletier, Jerry" uniqKey="Pelletier J" first="Jerry" last="Pelletier">Jerry Pelletier</name><name sortKey="Robert, Francis" sort="Robert, Francis" uniqKey="Robert F" first="Francis" last="Robert">Francis Robert</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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