R. L. Erikson

Comparison of oligonucleotides produced by RNase T1 digestion of 7 S RNA from avian and murine oncornaviruses and from uninfected cells

Abstract The 7 S RNA molecules isolated from Rous sarcoma virus (RSV), avian myeloblastosis virus (AMV), mouse sarcoma virus (MSV), and L cell virion (LCV) were treated with RNase T1, and the oligonucleotides produced were fractionated by two-dimensional electrophoresis. The 7 S RNAs from RSV and AMV yield identical fingerprints. Thirty-five oligonucleotides are observed in yields greater than 0.5 mole per mole RNA, and the molecules consist of about 280 nucleotides. LCV and MSV 7 S RNAs show a difference of two oligonucleotides of a total of 37. Comparison of avian and murine 7 S RNAs also shows a large number of similarities, including the 3′ terminus (U 4 C 2 )X OH . The results indicate that large portions of the sequence of 7 S oncornavirus RNAs have been conserved among viruses that replicate in different hosts. Analysis of 7 S RNA from uninfected chick fibroblasts demonstrates that they contain the same molecule as that found in AMV and RSV.

Antigenic and structural studies on the transforming proteins of rous sarcoma virus and yamaguchi 73 avian sarcoma virus

A widely cross reactive antiserum raised against denatured pp60v-src, the transforming protein encoded by Rous sarcoma virus, was used to test antigenic relationships with the transforming gene products encoded by other avian sarcoma viruses. The results showed that P90gag-yes, the transforming protein of a representative of Class III avian sarcoma viruses, is antigenically related to pp60v-src. Tryptic phosphopeptide analysis of P90gag-yes revealed two phosphotyrosine-containing peptides and one phosphoserine-containing peptide. One of the phosphotyrosine-containing peptides comigrated with the phosphotyrosine-containing tryptic peptide from pp60v-src.