title: Changes in the nuclear distribution of cyclin (PCNA) during S-phase are not triggered by post-translational modifications that are expected to moderately affect its charge.
abstract: Indirect immunofluorescence studies of HeLa cells using PCNA autoantibodies specific for cyclin have revealed striking changes in the nuclear localization of this protein during S-phase. Two-dimensional gel electrophoretic analysis of the [32P]orthophosphate and [35S]methionine labelled proteins from synchronized cells showed that phosphorylation, or other post-translational modifications that are expected to moderately affect the charge of cyclin (acetylation, glycosylation, sialylation, etc.) are not likely part of the mechanism(s) triggering the migration of this protein.
authors.forename: R
authors.initials: R
authors.lastname: Bravo
authors.forename: J E
authors.initials: JE
authors.lastname: Celis
mesh_terms: D002467:Cell Nucleus / Q000378:metabolism*; D004586:Electrophoresis; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D007399:Interphase; D008715:Methionine / Q000378:metabolism; D009698:Nucleoproteins / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D018809:Proliferating Cell Nuclear Antigen; D011499:Protein Processing, Post-Translational
chemical_list: D009698:Nucleoproteins; D010710:Phosphates; D018809:Proliferating Cell Nuclear Antigen; D008715:Methionine