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Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity

Xiuna Yang1, Masahiro Morita, Hui Wang

  • 1Laboratory of Structural Biology, Tsinghua University, Beijing, China.

Nucleic Acids Research
|November 1, 2008
PubMed

Insights

BTG2 protein regulates CAF1 deadenylase activity, impacting mRNA processing. This study reveals the BTG2-CAF1 complex structure and BTG2

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Structure

Background:

  • BTG2 is a transcriptional co-regulator involved in cell growth, differentiation, and DNA repair.
  • BTG2 interacts with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), components of the CCR4/NOT transcription complex.
  • CAF1 and POP2 are nucleases crucial for mRNA deadenylation.

Purpose of the Study:

  • To determine the crystal structures of human BTG2 and mouse TIS21.
  • To elucidate the interaction between BTG2 and CAF1.
  • To investigate the role of BTG2 in regulating CAF1 deadenylase activity.

Main Methods:

  • X-ray crystallography to obtain high-resolution structures of BTG2 and TIS21.
  • Site-directed mutagenesis to disrupt the BTG2-CAF1 interaction.
  • In vitro deadenylase assays using wild-type and mutant BTG2.

Main Results:

  • Crystal structures of human BTG2 (2.3 A) and mouse TIS21 (2.2 A) were determined.
  • A putative CAF1 binding site on BTG2 was identified.
  • BTG2 was found to suppress CAF1 deadenylase activity, with mutations disrupting the interaction abolishing this effect.

Conclusions:

  • The study provides structural insights into the BTG2-CAF1 complex formation.
  • BTG2 plays a suppressive role in regulating CAF1 deadenylase activity.
  • This work sheds light on the potential function of BTG2 in mRNA processing regulation.

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