Relationship of phosphorylation to the oligomerization of SV40 T antigen and its association with p53

FEBS Letters

Henning, Roland¹  Montenarh, Mathias¹  Stürzbecher, Horst-Werner¹  Mörike, Martin¹ 

[1] Department of Biochemistry, University of Ulm. PO Box 4066, D- 7900 Ulm (Donau, FRG

关键词: SV40 large Tantigen;    Oligomerization;    Phosphorylation;    T antigen-p53 complex;    Alkaline phosphatase;   

DOI  :  10.1016/0014-5793(85)81087-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The potential significance of the phosphorylation of SV40 large T antigen for oligomers and complexes with the cellular protein p53 was investigated. We observed that T antigen oligomers remain stable after enzymatic dephosphorylation by alkaline phosphatase up to 80%. Separate analysis of free and p53-bound T antigen revealed a considerably lower phosphorylation of the p53-bound subclass. Therefore, a simple correlation between the overall phosphorylation of T antigen and the formation of oligomers and T-p53 complexes is highly unlikely.

【 授权许可】

Unknown