title: Polyphosphate as a source of phosphoryl group in protein modification in the archaebacterium Sulfolobus acidocaldarius.
abstract: The incubation of polyphosphates with the ribosomal fraction of Sulfolobus acidocaldarius leads to the covalent attachment of phosphate to threonine residue(s) of a single 40,000 Mr protein. The hydrolysis kinetics of this protein showed that polyphosphate might be the modifying group. The reaction requires 2 mM Mn2+ ions and is time-dependent. ATP strongly inhibits the transfer of phosphate from polyphosphate, indicating that this process is catalyzed by an enzyme differing from the well-known protein kinases.
authors.affiliation: Institute of Microbiology, Regensburg University, FRG.
authors.forename: R
authors.initials: R
authors.lastname: Skorko
mesh_terms: D001105:Archaea / Q000187:drug effects / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism*; D006868:Hydrolysis; D010766:Phosphorylation; D011122:Polyphosphates / Q000493:pharmacokinetics*; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism
chemical_list: D011122:Polyphosphates; D011494:Protein Kinases