title: Cellular localization of the Escherichia coli SpoT protein.
abstract: The SpoT protein of Escherichia coli serves as a source of degradation as well as an apparent source of synthesis of (p)ppGpp. Since the subcellular localization of SpoT might be a clue to its function, we have used SpoT-specific antisera to analyze cell extracts fractionated on sucrose gradients. We find that the SpoT protein is not bound to ribosomes or to either inner or outer membrane fractions. Although the SpoT protein is found in large aggregates, its localization is probably cytosolic.
authors.affiliation: Section on Molecular Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: D R
authors.initials: DR
authors.lastname: Gentry
authors.forename: M
authors.initials: M
authors.lastname: Cashel
mesh_terms: D002451:Cell Compartmentation; D002458:Cell Fractionation; D003600:Cytosol; D004926:Escherichia coli / Q000502:physiology*; D008566:Membranes / Q000737:chemistry; D011755:Pyrophosphatases / Q000302:isolation & purification*
chemical_list: C027627:guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase; D011755:Pyrophosphatases