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Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein

Seung Hwan Lee1, Jungsic Oh, Jonghyun Park

  • 1School of Interdisciplinary Bioscience & Bioengineering, Pohang University of Science & Technology (POSTECH), Pohang 790-784, Korea, Department of Physics, Pohang University of Science & Technology (POSTECH), Pohang 790-784, Korea, Department of Life Sciences, Pohang University of Science & Technology (POSTECH), Pohang 790-784, Korea and Division of Integrative Biosciences & Biotechnology, Pohang University of Science & Technology (POSTECH), Pohang 790-784, Korea.

Nucleic Acids Research
|December 3, 2013
PubMed

Insights

Poly(A)-binding protein (PABP) changes shape upon binding to mRNA's poly(A) tail, influencing translation and stability. Interactions with other proteins, like PABP-interacting protein 2, alter PABP's conformation, regulating its function.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Poly(A)-binding protein (PABP) is crucial for mRNA translation and stability.
  • PABP interacts with numerous proteins via the 3' poly(A) tail of mRNA.

Purpose of the Study:

  • To visualize PABP in real-time and understand its conformational changes upon poly(A) binding.
  • To elucidate the role of PABP-interacting protein 2 in modulating PABP conformation and function.

Main Methods:

  • Real-time single-molecule visualization of PABP.
  • Analysis of PABP structure and its interactions with poly(A) and effector proteins.

Main Results:

  • PABP adopts a bent conformation (RRM1 near RRM4) when bound to poly(A), due to bending between RRM2 and RRM3.
  • PABP-interacting protein 2 disrupts this bent structure, inhibiting PABP-poly(A) binding.
  • Conformational changes in PABP are critical for its regulatory functions.

Conclusions:

  • PABP's conformation is dynamically regulated by its interactions with molecules like poly(A) and PABP-interacting protein 2.
  • These conformational dynamics are key to PABP's role in modulating mRNA translation and stability.

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