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An engineered RNA binding protein with improved splicing regulation.

Melissa A Hale1,2, Jared I Richardson1,2, Ryan C Day1,2

  • 1Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA.

Nucleic Acids Research
|January 9, 2018
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Summary

Synthetic muscleblind-like (MBNL) proteins were engineered to investigate alternative splicing regulation. Domain-specific MBNL variants showed altered splicing activity, suggesting therapeutic potential for myotonic dystrophy.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Biochemistry

Background:

  • Muscleblind-like (MBNL) proteins regulate alternative splicing during development.
  • MBNL sequestration by CUG/CCUG repeats causes myotonic dystrophy (DM).
  • MBNL1 protein has two tandem RNA binding domains (ZF1-2 and ZF3-4) that recognize YGCY motifs.

Purpose of the Study:

  • To determine functional differences between MBNL1's RNA binding domains.
  • To engineer synthetic MBNL proteins (MBNL-AA, MBNL-BB) with duplicated domains.
  • To assess the impact of domain duplication on splicing regulation and RNA binding.

Main Methods:

  • Construction and characterization of synthetic MBNL proteins (MBNL-AA, MBNL-BB).
  • Splicing regulation assays to measure protein activity.
  • RNA binding analysis to determine specificity and affinity.

Main Results:

  • MBNL-AA exhibited up to 5-fold increased splicing activity; MBNL-BB showed 4-fold decreased activity.
  • Differences in splicing activity correlated with altered RNA binding specificities, not affinity.
  • ZF1-2 domain drives splicing regulation via YGCY motif recognition; ZF3-4 acts as a general RNA binder.

Conclusions:

  • The two RNA binding domains of MBNL1 possess distinct functions.
  • Synthetic MBNL proteins can be engineered for altered splicing activity.
  • Engineered MBNL proteins show promise as research tools and potential therapeutics for DM and related diseases.