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XB-ART-18538
J Mol Biol 1996 Feb 16;2561:20-30. doi: 10.1006/jmbi.1996.0065.
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Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction.

Kühn U , Pieler T .


Abstract
Subsets of the four RNA binding domains (RBD 1 to 4) in the Xenopus poly-adenylate binding protein (PABP) have distinct affinities and specificities for RNA. RBDs 1 plus 2 exhibit RNA affinity and selectivity equal to the wild-type (WT) protein. RBDs 3 plus 4 have distinct selectivity and about ten-fold reduced affinity for A23, and the isolated RBDs 2 or 3 or 4 exhibit about 100-fold reduced affinity for A23 in comparison to WT. For the full-length protein, independent RNA contacts have been mapped by UV crosslinking with RBDs 1/2 and RBDs 3/4. The carboxy-terminal, non-RBD portion of the protein does not contribute to RNA affinity or selectivity, but confers homodimerization activity on PABP. RBDs 3 and 4 cooperate with the C terminus to gain poly(A) organizing activity, i.e. the ability to form an RNP with multiple, regularly spaced copies of PABP on a poly(A) substrate.

PubMed ID: 8609610
Article link: J Mol Biol


Species referenced: Xenopus
Genes referenced: pabpc1 pabpc4