Premium
Characterization of the RNA‐binding Motif of Phosphoglycerate Kinase 1 – a Moonlighting Function for a Metabolic Enzyme
Author(s) -
Walker Austin,
Friend Kyle
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.592.1
Subject(s) - phosphoglycerate kinase , enzyme , biochemistry , rna , biology , binding site , glycolysis , nucleotide , chemistry , gene
Phosphoglycerate Kinase 1 (PGK1) is an enzyme that plays an integral role in glucose metabolism, catalyzing the reaction that converts 1,3‐bisphosphoglycerate into 3‐phosphoglycerate in glycolysis, and the reverse reaction in gluconeogenesis. In addition, PGK1 has been shown to have an RNA binding activity. This suggests that, in addition to its role in metabolism, PGK1 “moonlights” as a RNA‐regulatory enzyme. In particular, PGK1 was shown to down‐regulate the expression of the mRNAs which it bound. The goal of the current study is to identify the RNA sequence(s) that binds PGK1, using the Systematic Evolution of Ligands by Exponential Enrichment (SELEX) technique. By identifying PGK1's consensus sequence, we will further elucidate the role of the enzyme in the cell beyond its metabolic capabilities, perhaps uncovering a new layer of regulation. We will then test how well PGK1 binds these RNA sequences via fluorescence polarization. Support or Funding Information Dr. G. Ashley Allen ‘65 Students Research Grant Fund, Washington and Lee University Chemistry and Biochemistry Department, Lenfest Grant