Abstract
The C-terminal domain of poly(A)-binding protein (PABC) is a peptide-binding domain found in poly(A)-binding proteins (PABPs) and a HECT (homologous to E6-AP C-terminus) family E3 ubiquitin ligase. In protein synthesis, the PABC domain of PABP functions to recruit several translation factors possessing the PABP-interacting motif 2 (PAM2) to the mRNA poly(A) tail. We have determined the solution structure of the human PABC domain in complex with two peptides from PABP-interacting protein-1 (Paip1) and Paip2. The structures show a novel mode of peptide recognition, in which the peptide binds as a pair of beta-turns with extensive hydrophobic, electrostatic and aromatic stacking interactions. Mutagenesis of PABC and peptide residues was used to identify key protein-peptide interactions and quantified by isothermal calorimetry, surface plasmon resonance and GST pull-down assays. The results provide insight into the specificity of PABC in mediating PABP-protein interactions.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Conserved Sequence
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Humans
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Hydrophobic and Hydrophilic Interactions
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Peptide Initiation Factors / chemistry
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Peptide Initiation Factors / metabolism
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Peptides / chemistry
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Peptides / metabolism
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Poly(A)-Binding Proteins / chemistry*
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Poly(A)-Binding Proteins / metabolism
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Protein Binding
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Protein Conformation
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Protein Structure, Tertiary
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RNA-Binding Proteins
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Repressor Proteins
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Ribosomal Proteins / chemistry*
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Static Electricity
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Ubiquitin-Protein Ligases / chemistry*
Substances
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Carrier Proteins
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Ligands
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PAIP1 protein, human
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PAIP2 protein, human
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Peptide Initiation Factors
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Peptides
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Poly(A)-Binding Proteins
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RNA-Binding Proteins
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Repressor Proteins
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Ribosomal Proteins
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UBR5 protein, human
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Ubiquitin-Protein Ligases