Structural insights into RNA recognition properties of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae

IUBMB Life. 2014 Sep;66(9):631-8. doi: 10.1002/iub.1313. Epub 2014 Oct 6.

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC: 1.2.1.12) is an essential enzyme in the glycolytic pathway. However, recent evidence demonstrates that GAPDH displays a range of new functions unrelated to its glycolytic function. GAPDH has long been known as a 3' AU-rich element-binding protein; however, its RNA recognition mechanism is still not well understood. Here, we present the first crystal structure of GAPDH3 from Saccharomyces cerevisiae and identify its RNA-binding specificity and propose an RNA recognition model based on structural and biochemical studies. This study sheds light on the RNA-binding mechanism of GAPDH3 and contributes to a better understanding of the molecular mechanisms of its RNA-related functions.

Keywords: GAPDH3; RNA binding; RNA recognition model; crystal structure; sequence specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fluorescence Polarization
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
  • Models, Molecular*
  • Protein Binding
  • Protein Conformation
  • RNA / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Substrate Specificity

Substances

  • RNA
  • Glyceraldehyde-3-Phosphate Dehydrogenases