The phosphorylation at Thr 124 of simian virus 40 large T antigen is crucial for its oligomerization.

Abstract:

:SV40 large T antigen is phosphorylated at up to ten different amino acids clustered in an N-terminal and a C-terminal part of the polypeptide chain. The N-terminal phosphorylated residues include Ser 123 and Thr 124. We have analyzed the oligomerization, the complex formation with the cellular oncoprotein p53 and the DNA-binding properties of T antigen from two different SV40 transformed cell lines which have either an amino acid exchange at Ser 123 to Phe (W7) or Thr 124 to Ile (D29). In comparison to wild-type T antigen both mutant T antigens have a slightly reduced binding affinity for both binding sites, I and II, of SV40 DNA. Phosphorylation at both residues of T antigen is not essential for formation of the complex with p53. Only the phosphorylation at Thr 124 seems to be critical for the formation of high molecular mass oligomers. Our data support the hypothesis that the oligomerization of T antigen seems to be implicated in viral DNA replication.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Montenarh M,Müller D

doi

10.1016/0014-5793(87)80925-0

subject

Has Abstract

pub_date

1987-09-14 00:00:00

pages

199-204

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)80925-0

journal_volume

221

pub_type

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