title: Binding of adenylate kinase to RNA.
abstract: Adenylate kinase (ATP:AMP transphosphorylase) is a key enzyme in energy metabolism. The activity of its isoforms is subjected to multiple regulations. It is shown here that a specific fraction consisting of all adenylate kinase isoforms from tobacco leaves and tissue cultures does not bind to the anionic exchange-resin Mono Q. Sample pretreatment with ribonuclease could restore full binding to Mono Q, suggesting an association of adenylate kinase with RNA similar to the enzyme of Chenopodium rubrum (J. Chromatogr. 625: 13-19). We propose here that at least in vitro adenylate kinase can behave as an RNA-binding protein and that RNA-binding of adenylate kinase isoforms may be related to regulatory mechanisms.
authors.affiliation: Lab. Biochimie et Physiologie Végétales, Université de Genève, Switzerland.
authors.forename: U
authors.initials: U
authors.lastname: Schlattner
authors.forename: E
authors.initials: E
authors.lastname: Wagner
authors.forename: H
authors.initials: H
authors.lastname: Greppin
authors.forename: M
authors.initials: M
authors.lastname: Bonzon
mesh_terms: D000263:Adenylate Kinase / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D007527:Isoenzymes / Q000378:metabolism; D010947:Plants, Toxic; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D014026:Nicotiana / Q000201:enzymology
chemical_list: D007527:Isoenzymes; D016601:RNA-Binding Proteins; D012313:RNA; D000263:Adenylate Kinase