title: Structural insights into RNA recognition properties of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae.
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.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Hui
authors.initials: H
authors.lastname: Shen
authors.forename: Hong
authors.initials: H
authors.lastname: Wang
authors.forename: Qiao
authors.initials: Q
authors.lastname: Liu
authors.forename: Huihui
authors.initials: H
authors.lastname: Liu
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.forename: Xu
authors.initials: X
authors.lastname: Li
mesh_terms: D005454:Fluorescence Polarization; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012313:RNA / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D012313:RNA; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
keywords: GAPDH3; RNA binding; RNA recognition model; crystal structure; sequence specificity