PolyAC-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein. |
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| SMART accession number: | SM00517
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| Description: |
Involved in homodimerisation (either directly or indirectly) |
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| Interpro abstract (IPR002004): |
The polyadenylate-binding protein (PABP) has a conserved C-terminal domain (PABC), which is also found in the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains (IPR000569) [(PUBMED:11287654)]. PABP recognises the 3' mRNA poly(A) tail and plays an essential role in eukaryotic translation initiation and mRNA stabilisation/degradation. PABC domains of PABP are peptide-binding domains that mediate PABP homo-oligomerisation and protein-protein interactions. In mammals, the PABC domain of PABP functions to recruit several different translation factors to the mRNA poly(A) tail [(PUBMED:11940585)].
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| GO function: | RNA binding (GO:0003723) |
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| Family alignment: |
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There are 390
PolyA domains in 378 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Kuhn U, Pieler T
- Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction.
- J Mol Biol. 1996; 256: 20-30
- Display 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.
- Wormington M, Searfoss AM, Hurney CA
- Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes.
- EMBO J. 1996; 15: 900-9
- Display abstract
The translational regulation of maternal mRNAs is the primary mechanism by which stage-specific programs of protein synthesis are executed during early development. Translation of a variety of maternal mRNAs requires either the maintenance or cytoplasmic elongation of a 3' poly(A) tail. Conversely, deadenylation results in translational inactivation. Although its precise function remains to be elucidated, the highly conserved poly(A) binding protein I (PABP) mediates poly(A)-dependent events in translation initiation and mRNA stability. Xenopus oocytes contain less than one PABP per poly(A) binding site suggesting that the translation of maternal mRNAs could be either limited by or independent of PABP. In this report, we have analyzed the effects of overexpressing PABP on the regulation of mRNAs during Xenopus oocyte maturation. Increased levels of PABP prevent the maturation-specific deadenylation and translational inactivation of maternal mRNAS that lack cytoplasmic polyadenylation elements. Overexpression of PABP does not interfere with maturation-specific polyadenylation, but reduces the recruitment of some mRNAs onto polysomes. Deletion of the C-terminal basic region and a single RNP motif from PABP significantly reduces both its binding to polyadenylated RNA in vivo and its ability to prevent deadenylation. In contrast to a yeast PABP-dependent poly(A) nuclease, PABP inhibits Xenopus oocyte deadenylase in vitro. These results indicate that maturation-specific deadenylation in Xenopus oocytes is facilitated by a low level of PABP consistent with a primary function for PABP to confer poly(A) stability.
- Structure (3D structures containing this domain)
3D Structures of PolyA domains in PDB
| PDB code | Main view | Title | | 1g9l |  | Solution structure of the pabc domain of human poly(a) binding protein |
| 1i2t |  | X-ray structure of the human hyperplastic discs protein: an ortholog of the c-terminal domain of poly(a)-binding protein |
| 1ifw |  | Solution structure of c-terminal domain of poly(a) binding protein from saccharomyces cerevisiae |
| 1jgn |  | Solution structure of the c-terminal pabc domain of human poly(a)-binding protein in complex with the peptide from paip2 |
| 1jh4 |  | Solution structure of the c-terminal pabc domain of human poly(a)-binding protein in complex with the peptide from paip1 |
| 1nmr |  | Solution structure of c-terminal domain from trypanosoma cruzi poly(a)-binding protein |
| 2dyd |  | Solution structure of the pabc domain from triticum aevestium poly(a)-binding protein |
- Links (links to other resources describing this domain)
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