FEBS Letters · 2004 · 12 citations · 17 references
Life SciencesBiochemistryNeuroscienceMolecular NeurobiologyMolecular NeuroscienceProtein-protein InteractionsLigand BindingNoncoding Rna BiologyProtein-nucleic Acid InteractionsRna PolyadenylationRna-binding ProteinsRna-protein InteractionsBinding StudiesNeuronal Rna-binding ProteinsPoly(a)-binding ProteinsProtein-rna Recognition MotifsRna MotifsRna Recognition MotifsRna-binding MotifRna-protein Recognition
Vasopressin (VP) mRNA and the non-coding BC200 RNA are sorted to neuronal dendrites. Among proteins interacting specifically with both RNAs is the multifunctional poly(A)-binding protein (PABP) consisting of four RNA recognition motifs (RRMs) and a C-terminal auxiliary domain. The protein/RNA interaction studies presented here reveal that PABPs association with VP- and BC200 RNA is exclusively mediated by RRMs 3+4. Quantitative binding studies with PABP deletion mutants demonstrate preferential binding of RRMs 3+4 even to poly(A)-homopolymers, while RRMs 1+2 exhibit a lower affinity for those sequences. An optimal interaction with both poly(A)- and non-poly(A) sequences is only achieved by full-size PABP.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations