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Mol Cell Biol. 1982 December; 2(12): 1463-1471
Copyright © 1982, American Society for Microbiology. All Rights Reserved.

New Properties of Simian Virus 40 Large T Antigen

Roland Seif

1 Laboratoire d'Enzymologie, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France

ABSTRACT

An 8,000-molecular-weight (8K) T antigen was found in all cells transformed by simian virus 40. The 8K T antigen was weakly labeled in vivo with [35S]methionine or 32Pi. A deletion in the human papovavirus BK genome, in the region coding for the carboxy-terminal end of the large T antigen, reduced the size of the 8K T antigen. The last 80 amino acids of the large T antigen include the sequence Asp-Asp-Asp-Asp unique to the activation peptide of trypsinogen. Large T antigen bound diisopropyl fluorophosphate and was retained by D-phenylalanine coupled to Sepharose beads, an affinity adsorbent that can retain chymotrypsin. The large T antigen and the recA protein of Escherichia coli, a known protease, have several properties in common as well as several similar sequences. Antibodies against large T antigen interacted with native recA protein.

Mol Cell Biol. 1982 December; 2(12): 1463-1471
Copyright © 1982, American Society for Microbiology. All Rights Reserved.



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Copyright © 1982 by the American Society for Microbiology. All rights reserved.