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Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
- Publication Year :
- 1997
-
Abstract
- Assembly of hepadnaviruses depends on the formation of a ribonucleoprotein (RNP) complex comprising the viral polymerase polypeptide and an RNA segment, epsilon, present on pregenomic RNA. This interaction, in turn, activates the reverse transcription reaction, which is primed by a tyrosine residue on the polymerase. We have shown recently that the formation of this RNP complex in an avian hepadnavirus, the duck hepatitis B virus, depends on cellular factors that include the heat shock protein 90 (Hsp90). We now report that RNP formation also requires ATP hydrolysis and the function of p23, a recently identified chaperone partner for Hsp90. Furthermore, we also provide evidence that the chaperone complex is incorporated into the viral nucleocapsids in a polymerase-dependent reaction. Based on these findings, we propose a model for hepadnavirus assembly and priming of viral DNA synthesis where a dynamic, energy-driven process, mediated by a multi-component chaperone complex consisting of Hsp90, p23 and, potentially, additional factors, maintains the reverse transcriptase in a specific conformation that is competent for RNA packaging and protein priming of viral DNA synthesis.
- Subjects :
- Chaperonins
viruses
Biology
General Biochemistry, Genetics and Molecular Biology
Cell Line
Hepatitis B Virus, Duck
Adenosine Triphosphate
Tumor Cells, Cultured
Animals
Humans
HSP90 Heat-Shock Proteins
Nucleocapsid
Molecular Biology
Polymerase
Ribonucleoprotein
Prostaglandin-E Synthases
General Immunology and Microbiology
General Neuroscience
RNA-Directed DNA Polymerase
Virus Assembly
RNA
Phosphoproteins
Molecular biology
Reverse transcriptase
Recombinant Proteins
Cell biology
Chaperone (protein)
DNA, Viral
biology.protein
Chaperone complex
Hepadnavirus
RNA, Viral
Chickens
Research Article
Molecular Chaperones
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....4f180550a8025a3a0a6059fcb82a596f