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Structural insights into RNA recognition properties of glyceraldehyde‐3‐phosphate dehydrogenase 3 from Saccharomyces cerevisiae
Author(s) -
Shen Hui,
Wang Hong,
Liu Qiao,
Liu Huihui,
Teng Maikun,
Li Xu
Publication year - 2014
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1313
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , saccharomyces cerevisiae , rna , biochemistry , dehydrogenase , enzyme , rna binding protein , biology , yeast , chemistry , microbiology and biotechnology , gene
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. © 2014 IUBMB Life, 66(9):631–638, 2014