Recognition of polyadenylate RNA by the poly(A)-binding protein

Rahul C. Deo, Jeffrey B. Bonanno, Nahum Sonenberg, Stephen K. Burley

Research output: Contribution to journalArticle

370 Citations (Scopus)

Abstract

The cocrystal structure of human poly(A)-binding protein (PABP) has been determined at 2.6 Å resolution. PABP recognizes the 3' mRNA poly(A) tail and plays critical roles in eukaryotic translation initiation and mRNA stabilization/degradation. The minimal PABP used in this study consists of the N-terminal two RRM-type RNA-binding domains connected by a short linker (RRM1/2). These two RRMs form a continuous RNA-binding trough, lined by an antiparallel β sheet backed by four α helices. The polyadenylate RNA adopts an extended conformation running the length of the molecular trough. Adenine recognition is primarily mediated by contacts with conserved residues found in the RNP motifs of the two RRMs. The convex dorsum of RRM1/2 displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with translation initiation factors and regulatory proteins.

Original languageEnglish (US)
Pages (from-to)835-845
Number of pages11
JournalCell
Volume98
Issue number6
DOIs
StatePublished - Sep 17 1999
Externally publishedYes

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Poly(A)-Binding Proteins
RNA
Peptide Initiation Factors
Messenger RNA
RNA Stability
Adenine
Running
Conformations
Stabilization
Display devices
Degradation
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Recognition of polyadenylate RNA by the poly(A)-binding protein. / Deo, Rahul C.; Bonanno, Jeffrey B.; Sonenberg, Nahum; Burley, Stephen K.

In: Cell, Vol. 98, No. 6, 17.09.1999, p. 835-845.

Research output: Contribution to journalArticle

Deo, Rahul C. ; Bonanno, Jeffrey B. ; Sonenberg, Nahum ; Burley, Stephen K. / Recognition of polyadenylate RNA by the poly(A)-binding protein. In: Cell. 1999 ; Vol. 98, No. 6. pp. 835-845.
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