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Updated: Sep 4, 2026

Amplification, Next-generation Sequencing, and Genomic DNA Mapping of Retroviral Integration Sites
Published on: March 22, 2016
A subset of Pr65gag is nucleus associated in murine leukemia virus-infected cells
M A Nash1, M K Meyer, G L Decker
1Department of Molecular Pathology, University of Texas M. D. Anderson Cancer Center, Houston 77030.
Abstract:
Nuclei of cells infected with Moloney murine leukemia virus (MoMuLV) were examined for the presence of gag proteins. This analysis was performed in conjunction with other studies suggesting a possible role for gag proteins in regulating nuclear events relating to processing and/or transport of viral genomic RNA. We detected Pr65gag and a p30-related protein in a nuclear fraction of infected cells. We also found evidence that a highly conserved amino acid sequence, which is shared by p30 and U1 small nuclear ribonucleoprotein 70-kDa protein, is a component of the nuclear targeting sequence for Pr65gag. Immunoelectron microscopy studies with a monoclonal anti-p12 antibody established that approximately 18% of gag-containing proteins of MoMuLV are located in the nucleus. Such gag-containing proteins from a mutant MoMuLV that lacks N-terminal myristic acid had greater affinity for the nucleus, suggesting that fatty acid acylation of Pr65gag plays a role in overcoming the proposed nuclear transport signal. The possible roles that nuclear gag proteins may play in retroviral replication are discussed.
Insights
Moloney murine leukemia virus (MoMuLV) gag proteins were found in infected cell nuclei. Fatty acid acylation of these proteins may regulate their nuclear transport, impacting retroviral replication.
Area of Science:
- Retroviral Biology
- Molecular Virology
- Cellular Biology
Background:
- Moloney murine leukemia virus (MoMuLV) is a retrovirus.
- Viral gag proteins are essential structural components.
- The role of gag proteins in nuclear events is under investigation.
Purpose of the Study:
- To investigate the presence and function of MoMuLV gag proteins in the nucleus.
- To identify the nuclear targeting signals within gag proteins.
- To explore the influence of fatty acid acylation on gag protein nuclear localization.
Main Methods:
- Subcellular fractionation to isolate nuclear components.
- Detection of viral proteins using specific antibodies and immunoelectron microscopy.
- Analysis of protein sequences for conserved targeting motifs.
- Comparison of wild-type and mutant MoMuLV gag proteins lacking myristic acid.
Main Results:
- Pr65gag and a p30-related protein were detected in the nuclear fraction of MoMuLV-infected cells.
- A conserved amino acid sequence shared with U1 snRNP 70-kDa protein acts as a nuclear targeting signal for Pr65gag.
- Approximately 18% of gag-containing proteins were found in the nucleus.
- Mutant MoMuLV gag proteins lacking N-terminal myristic acid showed increased nuclear affinity.
Conclusions:
- MoMuLV gag proteins are present in the nucleus and may play a role in viral replication.
- Nuclear localization is mediated by a specific targeting sequence within gag proteins.
- Fatty acid acylation of Pr65gag appears to modulate its nuclear transport, potentially overcoming the nuclear import signal.
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