Studies on the function of polyadenylic acid on poliovirus RNA.
RNAase H was used to remove selectively over 83% of 3' terminal polyadenylic acid [poly(A)] from poliovirus RNA. In a single cycle infection with this poly(A)-deficient RNA, no evidence for multiplication of the RNA was found. To elucidate further the function of poliovirus poly (A), the translational capacity of the RNAase H-treated and untreated RNA was studied in a cell-free protein synthesizing system prepared from HeLa cells. Removal of most of the poly(A) did not affect the pattern or amount of polypeptides synthesized. We conclude that the poly(A) on poliovirus RNA is probably necessary to the replication of the molecule.
D002474:Cell-Free System; D004926:Escherichia coli / Q000201:enzymology; D006367:HeLa Cells; D010452:Peptide Biosynthesis; D017955:Poliovirus / Q000254:growth & development / Q000378:metabolism; D011061:Poly A / Q000378:metabolism*; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000096:biosynthesis* / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D014764:Viral Proteins / Q000096:biosynthesis; D014779:Virus Replication
D012367:RNA, Viral; D014764:Viral Proteins; D011061:Poly A; D012260:Ribonucleases