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ZIRC
ZFIN ID: ZDB-PUB-130710-83
Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins
von Moeller, H., Lerner, R., Ricciardi, A., Basquin, C., Marzluff, W.F., and Conti, E.
Date: 2013
Source: Nucleic acids research   41(16): 7960-71 (Journal)
Registered Authors:
Keywords: none
MeSH Terms:
  • Amino Acid Sequence
  • Animals
  • DEAD-box RNA Helicases/chemistry*
  • DEAD-box RNA Helicases/metabolism
  • Eukaryotic Initiation Factor-3/chemistry
  • Eukaryotic Initiation Factor-3/metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleocytoplasmic Transport Proteins/chemistry*
  • Nucleocytoplasmic Transport Proteins/metabolism
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • RNA-Binding Proteins/chemistry*
  • RNA-Binding Proteins/metabolism
  • Sequence Alignment
  • Zebrafish Proteins/chemistry*
  • Zebrafish Proteins/metabolism
PubMed: 23804756 Full text @ Nucleic Acids Res.
ABSTRACT

In metazoans, replication-dependent histone mRNAs end in a stem-loop structure instead of the poly(A) tail characteristic of all other mature mRNAs. This specialized 32 end is bound by stem-loop binding protein (SLBP), a protein that participates in the nuclear export and translation of histone mRNAs. The translational activity of SLBP is mediated by interaction with SLIP1, a middle domain of initiation factor 4G (MIF4G)-like protein that connects to translation initiation. We determined the 2.5 Å resolution crystal structure of zebrafish SLIP1 bound to the translation–activation domain of SLBP and identified the determinants of the recognition. We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5. We confirmed the binding of SLIP1 to DBP5 and eIF3g by pull-down assays and determined the 3.25 Å resolution structure of SLIP1 bound to the DBP5 SBM. The SBM-binding and homodimerization residues of SLIP1 are conserved in the MIF4G domain of CBP80/20-dependent translation initiation factor (CTIF). The results suggest how the SLIP1 homodimer or a SLIP1–CTIF heterodimer can function as platforms to bridge SLBP with SBM-containing proteins involved in different steps of mRNA metabolism.

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