title: A 57-kilodalton protein associated with Spiroplasma melliferum fibrils undergoes reversible phosphorylation.
abstract: Phosphorylation of a major 57-kilodalton protein substrate was observed in cell lysates of Spiroplasma melliferum BC3 incubated with [gamma-32P]ATP. Only serine phosphates have been isolated from the acid hydrolysate of the phosphorylated protein. The 57-kilodalton protein substrate was found, to a large extent, in the cytosolic fraction and, to a lesser extent, associated with cell membranes and was detected in the Triton X-100-insoluble fraction that contained fibrils.
authors.affiliation: Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
authors.forename: M W
authors.initials: MW
authors.lastname: Platt
authors.forename: J
authors.initials: J
authors.lastname: Reizer
authors.forename: S
authors.initials: S
authors.lastname: Rottem
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002465:Cell Movement; D008970:Molecular Weight; D015388:Organelles / Q000378:metabolism; D010750:Phosphoproteins / Q000302:isolation & purification; D010766:Phosphorylation; D013149:Spiroplasma / Q000378:metabolism* / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D010750:Phosphoproteins