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Histone mRNA translation in metazoans: SLIP1 as the bridging factor between the 5' and 3' utrs of the histone mRNA

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  1. Tez No: 400100
  2. Yazar: NİHAL GÜLSEREN ÇAKMAKÇI
  3. Danışmanlar: WİLLİAM F. MARZLUFF
  4. Tez Türü: Doktora
  5. Konular: Biyoloji, Biology
  6. Anahtar Kelimeler: Belirtilmemiş.
  7. Yıl: 2007
  8. Dil: İngilizce
  9. Üniversite: University of North Carolina at Chapel Hill
  10. Enstitü: Yurtdışı Enstitü
  11. Ana Bilim Dalı: Belirtilmemiş.
  12. Bilim Dalı: Belirtilmemiş.
  13. Sayfa Sayısı: 192

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Özet (Çeviri)

Histone proteins packages newly synthesized DNA into higher organizations. DuringDNA synthesis in metazoans, there is a high demand for biosynthesis of histone proteins.Strict regulation of histone protein expression in the S phase is achieved by unique structureof histone mRNA. Unlike other eukaryotic mRNAs, histone mRNAs end with a stem-loop,rather than a polyA tail. The stem-loop binds the stem loop binding protein (SLBP), a novelRNA binding protein that is conserved among metazoans. Xenopus laevis has two forms ofSLBP. xSLBP1 is the homolog of hSLBP and N-terminus of the both proteins are shown tostimulate translation of histone mRNA. xSLBP2, the oocyte specific form, maintains highsimilarity to hSLBP only in the RBD. xSLBP2 does not stimulate histone mRNA translation,but instead represses histone mRNAs during early oogenesis. xSLBP2 is degraded duringoocyte maturation, and then xSLBP1 binds histone mRNAs coinciding with the timing oftranslational activation. I have characterized a motif in the N-terminus of xSLBP1 andhSLBP which is responsible for translational activity. The motif, DWX(3-4)VEE, is highlyconserved among vertebrates. I demonstrated that this motif interacts with a novel factor,named as SLBP-Interacting Protein 1 (SLIP1). Interestingly, SLIP1 stimulates translation ofhistone mRNA to higher levels in the presence of SLBP. SLBP mutants that can notstimulate histone mRNA translation are also incapable of interacting with SLBP.Previously, it had been reported that eukaryotic polyadenylated mRNAs weretranslationally stimulated by circularization via protein-protein interactions. I showed thatSLIP1 interacts with translation initiation factors IF4GI and II. Possibly, histone mRNAforms a closed loop similar to polyadenylated mRNAs during translation. Together withJeremy Kupsco and Bob Duronio, I genetically investigated the role of SLBP and SLIP1 inDrosophila melanogaster. We identified a region in the N-terminus of dSLBP which has anessential post-processing function in Drosophila during early development. We demonstratedthat dSLIP1 interacts with dSLBP. We characterized the SLIP1 interaction motif in the Nterminusof SLBP, (KFX(2-3)VEKE), which is similar to DWX(3-4)VEE motif in vertebrates.Both dSLBP and SLIP1 null mutant flies are embryonically lethal, probably due to a defect intranslation of histone mRNAs. We conclude that the SLIP1-SLBP interaction is crucial forviability of Drosophila during early development.

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