title: Phosphorylation of SV40 large T antigen at threonine residues results in conversion to a lower apparent molecular weight form.
abstract: Simian virus 40 large T antigen (large T) was dephosphorylated with potato acid phosphatase at pH 5.5. Phosphate residues bound to serine were more susceptible to potato acid phosphatase than threonine-bound phosphate residues. Dephosphorylation of the threonine residues with potato acid phosphatase resulted in a reduced gel-electrophoretic mobility, while removal of the remaining phosphate groups had no effect on the mobility of large T. Pulse-chase experiments revealed a slower migrating form of newly synthesized large T which was converted by phosphorylation to a faster migrating form and had a half-life of approximately 1 h.
authors.affiliation: Department of Pathology, University of California, San Diego, La Jolla.
authors.forename: F A
authors.initials: FA
authors.lastname: Grässer
authors.forename: S
authors.initials: S
authors.lastname: König
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D000952:Antigens, Polyomavirus Transforming / Q000737:chemistry / Q000378:metabolism*; D002460:Cell Line; D015180:Electrophoresis, Gel, Two-Dimensional; D010766:Phosphorylation; D013539:Simian virus 40 / Q000276:immunology / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism*
chemical_list: D000952:Antigens, Polyomavirus Transforming; D013912:Threonine; D000135:Acid Phosphatase