A Protein Covalently Linked to Poliovirus Genome RNA

Poliovirion [32P]RNA, after digestion with RNase T2, yields mononucleotides and a labeled compound ``X,'' which is not negatively charged at pH 5. X contains, relative to the label in virion RNA, one to two phosphates and is partially acid insoluble. It can be labeled with tritiated amino...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1977-01, Vol.74 (1), p.59-63
Main Authors: Lee, Yuan Fon, Nomoto, Akio, Detjen, Barbara Morgan, Wimmer, Eckard
Format: Article
Language:English
Subjects:
Gels
Genomes
Messenger RNA
Molecular Weight
Nucleosides
Phosphates
Polio
Poliovirus
Poliovirus - ultrastructure
Ribonucleoproteins
RNA
RNA, Viral
Viral Proteins
Virions
Virus Replication
Viruses
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Summary:Poliovirion [32P]RNA, after digestion with RNase T2, yields mononucleotides and a labeled compound ``X,'' which is not negatively charged at pH 5. X contains, relative to the label in virion RNA, one to two phosphates and is partially acid insoluble. It can be labeled with tritiated amino acids 3 hr after infection, is insoluble in chloroform/methanol, and can be digested with Pronase. These observations suggest that X is a protein. The protein cannot be removed from the polio genome when the RNA is (i) sedimented through a sucrose gradient in 0.5 M NaCl, (ii) heated to 100 degrees in the presence of sodium dodecyl sulfate followed by sedimentation through a sucrose gradient in 80% dimethylsulfoxide, or (iii) banded in 4 M cesium trichloroacetate. Digestion of the32P-labeled protein with Pronase yields one major32P-labeled product, which contains pUp. The protein migrates faster than capsid protein VP4 in a polyacrylamide gel. Our data show that the genome of poliovirus, but not poliovirus mRNA [A. Nomoto, Y. F. Lee, and E. Wimmer (1976) Proc. Natl. Acad. Sci. USA 73, 375-380], is covalently attached to a small virus-coded protein (molecular weight
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.74.1.59