Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/99359
DC FieldValueLanguage
dc.contributor.authorTsai, Tsung-Linzh_TW
dc.contributor.authorLin, Ching-Houngzh_TW
dc.contributor.authorLin, Chao-Nanzh_TW
dc.contributor.authorLo, Chen-Yuzh_TW
dc.contributor.author吳弘毅zh_TW
dc.contributor.authorWu, Hung-Yizh_TW
dc.date2018-
dc.date.accessioned2020-02-04T03:35:17Z-
dc.date.available2020-02-04T03:35:17Z-
dc.identifier.urihttp://hdl.handle.net/11455/99359-
dc.description.abstractIn the present study, we investigated the roles of interactions among the poly(A) tail, coronavirus nucleocapsid (N) protein, and poly(A)-binding protein (PABP) in the regulation of coronavirus gene expression. Through dissociation constant (Kd ) comparison, we found that the coronavirus N protein can bind to the poly(A) tail with high affinity, establishing N protein as a PABP. A subsequent analysis with UV cross-linking and immunoprecipitation revealed that the N protein is able to bind to the poly(A) tail in infected cells. Further examination demonstrated that poly(A) tail binding by the N protein negatively regulates translation of coronaviral RNA and host mRNA both in vitro and in cells. Although the N protein can interact with PABP and eukaryotic initiation factor 4G (eIF4G), the poor interaction efficiency between the poly(A)-bound N protein and eIF4E may explain the observed decreased translation efficiency. In addition to interaction with translation factor eIF4G, the N protein is able to interact with coronavirus nonstructural protein 9 (nsp9), a replicase protein required for replication. The study demonstrates interactions among the poly(A) tail, N protein, and PABP both in vitro and in infected cells. Of the interactions, binding of the poly(A) tail to N protein decreases the interaction efficiency between the poly(A) tail and eIF4E, leading to translation inhibition. The poly(A)-dependent translation inhibition by N protein has not been previously demonstrated and thus extends our understanding of coronavirus gene expression.IMPORTANCE Gene expression in coronavirus is a complicated and dynamic process. In this study, we demonstrated that coronavirus N protein is able to bind to the poly(A) tail with high affinity, establishing N protein as a PABP. We also show how the interplay between coronavirus 3' poly(A) tail, PABP, and N protein regulates gene expression of the coronavirus and host cell. Of the interactions, poly(A) tail binding by the N protein negatively regulates translation, and to our knowledge, this inhibition of translation by binding of the N protein to poly(A) tail has not been previously studied. Accordingly, the study provides fundamental molecular details regarding coronavirus infection and expands our knowledge of coronavirus gene expression.zh_TW
dc.language.isoenzh_TW
dc.relationJournal of virology, Volume 92, Issue 23zh_TW
dc.subjectRNA synthesiszh_TW
dc.subjectcoronaviruszh_TW
dc.subjectgene expressionzh_TW
dc.subjectnucleocapsid proteinzh_TW
dc.subjectpoly(A) tailzh_TW
dc.subjectpoly(A)-binding proteinzh_TW
dc.subjectreplicationzh_TW
dc.subjecttranslationzh_TW
dc.subjectAnimalszh_TW
dc.subjectCattlezh_TW
dc.subjectCoronavirus Infectionszh_TW
dc.subjectCoronavirus, Bovinezh_TW
dc.subjectEukaryotic Initiation Factor-4Ezh_TW
dc.subjectEukaryotic Initiation Factor-4Gzh_TW
dc.subjectHEK293 Cellszh_TW
dc.subjectHumanszh_TW
dc.subjectNucleocapsid Proteinszh_TW
dc.subjectPoly Azh_TW
dc.subjectPoly(A)-Binding Proteinszh_TW
dc.subjectGene Expression Regulationzh_TW
dc.titleInterplay between the Poly(A) Tail, Poly(A)-Binding Protein, and Coronavirus Nucleocapsid Protein Regulates Gene Expression of Coronavirus and the Host Cellzh_TW
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1128/JVI.01162-18zh_TW
dc.awards2018zh_TW
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.fulltextwith fulltext-
item.languageiso639-1en-
item.grantfulltextrestricted-
Appears in Collections:獸醫病理生物學所
Files in This Item:
File Description SizeFormat Existing users please Login
372.pdf4.51 MBAdobe PDFThis file is only available in the university internal network    Request a copy
Show simple item record
 
TAIR Related Article

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.