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The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity

M Görlach1, C G Burd, G Dreyfuss

  • 1Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.

Experimental Cell Research
|April 1, 1994
PubMed
Summary

The poly(A)-binding protein (PABP) is abundant in the cytoplasm and binds strongly to poly(A) tails on mRNA. This suggests PABP may have additional roles beyond its known functions in mRNA stability and translation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Poly(A)-binding protein (PABP) interacts with the 3'-poly(A) tail of eukaryotic mRNA.
  • PABP and the poly(A) tail are crucial for mRNA stability and translation regulation.

Purpose of the Study:

  • To investigate the cellular localization, abundance, and RNA-binding properties of human PABP (hPABP).
  • To elucidate the role of hPABP in mRNA processing and regulation.

Main Methods:

  • Monoclonal antibodies were generated against hPABP.
  • Confocal immunofluorescence microscopy was used for cellular localization.
  • Quantitative immunoblotting assessed protein abundance and turnover.
  • In vitro selection/amplification assays determined RNA-binding affinities.

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Main Results:

  • hPABP exclusively localizes to the cytoplasm.
  • HeLa cells contain approximately 8 x 10^6 hPABP molecules per cell (approx. 4 microM concentration).
  • hPABP exhibits a low turnover rate and binds oligo(rA)25 with high affinity (Kd = 7 nM), with lower affinity for unrelated RNA (Kd > or = 0.5 microM).

Conclusions:

  • The high intracellular concentration of hPABP suggests a potential for binding to additional, lower-affinity sites in vivo.
  • The abundance of hPABP indicates a three-fold excess over cytoplasmic poly(A) binding sites.
  • These findings provide insights into the regulatory mechanisms of mRNA metabolism governed by PABP.