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Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site

Qin Yang1, Molly Coseno, Gregory M Gilmartin

  • 1Department of Microbiology and Molecular Genetics, University of Vermont, Stafford Hall, Burlington, VT 05405, USA.

Structure (London, England : 1993)
|February 8, 2011
PubMed

Insights

Cleavage factor I(m) (CFI(m)) uses its subunits to bind specific RNA sequences for mRNA 3' processing. This study reveals the crystal structure, showing how CFI(m)68 enhances RNA binding and promotes RNA looping.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • RNA Processing

Background:

  • Cleavage factor I(m) (CFI(m)) is crucial for eukaryotic mRNA 3' end processing.
  • It recognizes poly(A) sites via its subunits: CFI(m)25 (Nudix domain) and a larger subunit with an RNA recognition motif (RRM).
  • CFI(m)25 alone binds the UGUA element specifically.

Purpose of the Study:

  • To determine the crystal structure of the CFI(m)25/CFI(m)68 RRM/RNA complex.
  • To elucidate the structural basis for CFI(m)'s function in poly(A) site recognition and RNA looping.

Main Methods:

  • X-ray crystallography to obtain the complex structure.
  • Biochemical analysis to assess RNA binding and looping capabilities.

Main Results:

  • The crystal structure reveals a CFI(m)25 dimer clasped by two CFI(m)68 RRM domains.
  • Each CFI(m)25 subunit specifically binds a UGUA RNA element.
  • CFI(m)68 RRMs enhance RNA binding and facilitate RNA looping.

Conclusions:

  • The structure provides insights into CFI(m)'s mechanism of sequence-specific RNA binding.
  • CFI(m) possesses an intrinsic ability to direct RNA looping, potentially regulating alternative poly(A) site selection.

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