Assembly of avian reticuloendotheliosis virus: association of the core precursor polypeptide with the intracellular ribonucleoprotein complex.
AUTOR(ES)
Wong, T C
RESUMO
A virus-specific ribonucleoprotein complex is present in the cytoplasm of reticuloendotheliosis virus-transformed chicken bone marrow cells. This ribonucleoprotein complex contains viral reverse transcriptase activity and may represent a precursor to the budding virion. The major viral polypeptide associated with the ribonucleoprotein complex was a polypeptide with a molecular weight of 63,000. This protein exhibited a precursor-product relationship with the major reticuloendotheliosis virus structural core protein p29. Core polypeptides were not associated with the intracellular ribonucleoprotein complex. Thus, p29 was incorporated into the virion in the form of its precursor Pr63. The cleavage of Pr63 in the ribonucleoprotein complex was accomplished either during the budding process of shortly after the release of particles from the cell.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=288727Documentos Relacionados
- Avian reticuloendotheliosis virus: characterization of genome structure by heteroduplex mapping.
- Group-specific antigen shared by the members of the reticuloendotheliosis virus complex.
- Relationship of Reticuloendotheliosis Virus to the Avian Tumor Viruses: Nucleic Acid and Polypeptide Composition
- Assembly in an in vitro splicing reaction of a mouse insulin messenger RNA precursor into a 60-40S ribonucleoprotein complex.
- Avian reticuloendotheliosis virus: characterization of the high-molecular-weight viral RNA in transforming and helper virus populations.