Abstract
Simian virus 40 large tumor antigen was isolated by immunoaffinity chromatography from monkey or mouse cell cultures undergoing lytic or transforming infection. RNase-treated gel-purified large tumor antigen, on hydrolysis with alkali, gave about equimolar amounts of AMP, GMP, CMP, and UMP. Furthermore, RNA fragments of approximately 45 nucleotides could be isolated from large tumor antigen purified by the same procedure. Mapping of the T1 oligonucleotides showed a high complexity, as indicated by the presence of unique sequences of 15-30 nucleotides and of poly(A). This is compatible with the hypothesis that these RNA fragments are derived from cellular pre-mRNAs or mRNAs. Our results suggest that Simian virus 40 large tumor antigen is a RNA-binding protein and might possibly be involved in regulation of synthesis, maturation, or translation of cellular mRNAs.
MeSH Terms
Antigens, Neoplasm/analysis,isolation & purification
Antigens, Viral/analysis,isolation & purification
Antigens, Viral, Tumor
Carrier Proteins/analysis
Oligoribonucleotides/analysis
RNA/analysis
RNA, Messenger/metabolism
RNA-Binding Proteins
Simian virus 40/immunology
Chemicals
Antigens, Neoplasm
Antigens, Viral
Antigens, Viral, Tumor
Carrier Proteins
Oligoribonucleotides
RNA, Messenger
RNA-Binding Proteins
RNA
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Khandjian E W
Loche M
Darlix J L
Cramer R
Türler H
Weil R
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