Evidence that a central domain of nucleocapsid protein is required for RNA packaging in murine leukemia virus.

AUTOR(ES)

Rein, A

RESUMO

We have analyzed RNA packaging by a series of mutants altered in the nucleocapsid (NC) protein of Moloney murine leukemia virus (Mo-MuLV). We found that mutants lacking residues 8 through 11 or 44 through 60 of NC package Mo-MuLV RNA with virtually the same efficiency as wild-type Mo-MuLV. In contrast, point mutants altered at the conserved cysteines in the cysteine array (residues 26 and 29) and a mutant lacking residues 16 through 23 packaged Mo-MuLV RNA with approximately 1% of the efficiency of wild-type Mo-MuLV. The deficiency in packaged RNA was observed not only in Northern (RNA) analysis but also in an RNA-PCR assay, which would detect degraded as well as intact RNA. One of the cysteine array mutants was also shown to be defective with respect to encapsidation of hygromycin phosphotransferase mRNA containing a Mo-MuLV packaging signal. We suggest that a central region of NC, consisting of the cysteine array and flanking basic residues, is required for RNA packaging in Mo-MuLV.

Documentos Relacionados

• An amino-terminal domain of the Sendai virus nucleocapsid protein is required for template function in viral RNA synthesis.
• Role of Murine Leukemia Virus Nucleocapsid Protein in Virus Assembly
• Evidence that a downstream pseudoknot is required for translational read-through of the Moloney murine leukemia virus gag stop codon.
• The Nucleocapsid Domain Is Responsible for the Ability of Spleen Necrosis Virus (SNV) Gag Polyprotein To Package both SNV and Murine Leukemia Virus RNA
• Evidence that the packaging signal of Moloney murine leukemia virus extends into the gag region.