Yaciuk, P., Moran, E. (November 1991) Analysis with specific polyclonal antiserum indicates that the E1A-associated 300-kDa product is a stable nuclear phosphoprotein that undergoes cell cycle phase-specific modification. Mol Cell Biol, 11 (11). pp. 5389-97. ISSN 0270-7306 (Print)0270-7306 (Linking)
Abstract
Binding of a 300-kDa host cell protein (p300) is tightly correlated with the ability of the adenovirus E1A products to induce quiescent baby rat kidney cells to proliferate. We have generated rabbit polyclonal antibodies against p300 to characterize this protein further. We have found p300 to be a nuclear phosphoprotein that is actively synthesized in both quiescent and proliferating baby rat kidney cells. In partially purified mitotic cell populations, we observe a form of p300 with decreased electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels that shares a nearly identical partial proteolytic digest pattern with p300. The slower-migrating form of p300 is greatly reduced by treating immune complexes with potato acid phosphatase. The relative stability and presence of p300 even in resting cells suggests that p300 has a basal cell function, but the appearance of differentially modified forms during the cell cycle suggests the possibility that p300 function is modulated specifically in growing cells.
Item Type: | Paper |
---|---|
Uncontrolled Keywords: | Adenovirus Early Proteins Animals Antibodies Antibodies, Monoclonal Cell Cycle Cell Line Cell Line, Transformed Fluorescent Antibody Technique Half-Life HeLa Cells Humans Molecular Weight Nuclear Proteins/*metabolism Oncogene Proteins, Viral/analysis/*metabolism Phosphoproteins/*metabolism Rabbits/immunology Rats Sulfur Radioisotopes |
Subjects: | organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation |
CSHL Authors: | |
Communities: | CSHL labs |
Depositing User: | Matt Covey |
Date: | November 1991 |
Date Deposited: | 14 Jan 2016 16:56 |
Last Modified: | 14 Jan 2016 16:56 |
PMCID: | PMC361670 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32040 |
Actions (login required)
Administrator's edit/view item |