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The E5 oncoprotein of bovine papillomavirus binds to a 16 kd cellular protein.
Author(s) -
Goldstein D.J.,
Schlegel R.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08089.x
Subject(s) - biology , fusion protein , cancer , virus , microbiology and biotechnology , epitope , virology , antibody , biochemistry , immunology , gene , genetics , recombinant dna
The E5 oncoprotein of bovine papillomavirus type 1 is the smallest known viral transforming protein. It is a 44 amino acid polypeptide asymmetrically oriented in Golgi and plasma membranes which appears to modify (either directly or indirectly) the internalization and phosphorylation of at least two growth factor receptors: EGF and CSF‐1. To identify cellular proteins associated with E5, we have constructed two E5 fusion proteins, each of which contains a well‐characterized epitope at the E5 amino terminus. These E5‐epitope fusion proteins are biologically active, localize normally to cellular membranes and form dimers. Both monoclonal and polyclonal antibodies against the inserted epitopes specifically co‐precipitate E5 and an associated 16 kd cellular protein. A transformation‐defective E5 mutant containing a substitution within the hydrophobic portion of E5 is defective in its ability to bind the 16 kd protein. These findings suggest a role for E5/16 kd binding in the process of cellular transformation.