The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail.

@article{Keller2000TheNP,
  title={The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail.},
  author={Rebecca W Keller and Uwe Kuehn and Marcela Arag{\'o}n and L Bornikova and Elmar Wahle and David G. Bear},
  journal={Journal of molecular biology},
  year={2000},
  volume={297 3},
  pages={569-83}
}
The mammalian nuclear poly(A) binding protein, PABP2, controls the length of the newly synthesized poly(A) tail on messenger RNAs. To gain a better understanding of the mechanism of length control, we have investigated the structure of the PABP2.poly(A) complex. Electron microscopy and scanning force microscopy studies reveal that PABP2, when bound to poly(A), forms both linear filaments and discrete-sized, compact, oligomeric particles. The maximum diameter of the filament is 7 nm; the maximum… CONTINUE READING

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