Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2014 Jul 7:5:321.
doi: 10.3389/fpls.2014.00321. eCollection 2014.

Host and viral RNA-binding proteins involved in membrane targeting, replication and intercellular movement of plant RNA virus genomes

Affiliations
Review

Host and viral RNA-binding proteins involved in membrane targeting, replication and intercellular movement of plant RNA virus genomes

Kiwamu Hyodo et al. Front Plant Sci. .

Abstract

Many plant viruses have positive-strand RNA [(+)RNA] as their genome. Therefore, it is not surprising that RNA-binding proteins (RBPs) play important roles during (+)RNA virus infection in host plants. Increasing evidence demonstrates that viral and host RBPs play critical roles in multiple steps of the viral life cycle, including translation and replication of viral genomic RNAs, and their intra- and intercellular movement. Although studies focusing on the RNA-binding activities of viral and host proteins, and their associations with membrane targeting, and intercellular movement of viral genomes have been limited to a few viruses, these studies have provided important insights into the molecular mechanisms underlying the replication and movement of viral genomic RNAs. In this review, we briefly overview the currently defined roles of viral and host RBPs whose RNA-binding activity have been confirmed experimentally in association with their membrane targeting, and intercellular movement of plant RNA virus genomes.

Keywords: RNA replication; RNA virus; RNA-binding protein; cell-to-cell movement; cellular membrane.

PubMed Disclaimer

Figures

FIGURE 1
FIGURE 1
Schematic representation of the multiplication steps of a (+)RNA virus. Viral genomic RNA serves as the template for translation of the replicase proteins (vRdRp, viral RNA dependent RNA polymerase; vAP, auxiliary replicase protein). vAP recognizes vRNA in a sequence-specific manner and recruits to a selected membrane. vAP and vRdRp proteins interact with each other to form viral replication complexes (VRCs) with host proteins (HF) and vRNA (Step 1). Viral movement protein (MP) that is translated near the VRCs binds to vRNA. In the case of RCNMV, the MP expressed ectopically is recruited to the VRCs (Step 2; Kaido et al., 2009). MP binds to vRNA in or near the VRCs in a sequence non-specific manner and is transported to plasmodesmata (PD).

Similar articles

Cited by

References

    1. An M., Iwakawa H.-O., Mine A., Kaido M., Mise K., Okuno T. (2010). A Y-shaped RNA structure in the 3’ untranslated region together with the trans-activator and core promoter of Red clover necrotic mosaic virus RNA2 is required for its negative-strand RNA synthesis. Virology 405 100–109 10.1016/j.virol.2010.05.022 - DOI - PubMed
    1. Andreev I. G., Kim S. H., Kajinina N. O., Rakitina D. V., Fitzgerald A. G., Palukaitis P., et al. (2004). Molecular interactions between a plant virus movement protein and RNA: force spectroscopy investigation. J. Mol. Biol. 339 1041–1047 10.1016/j.jmb.2004.04.013 - DOI - PubMed
    1. Asurmendi S., Berg R. H., Koo J. C., Beachy R. N. (2004). Coat protein regulates formation of replication complexes during Tobacco mosaic virus infection. Proc. Natl. Acad. Sci. U.S.A. 101 1415–1420 10.1073/pnas.0307778101 - DOI - PMC - PubMed
    1. Baltz A. G., Munschauer M., Schwanhäusser B., Vasile A., Murakawa Y., Schueler M., et al. (2012). The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674–690 10.1016/j.molcel.2012.05.021 - DOI - PubMed
    1. Bamunusinghe D., Hemenway C. L., Nelson R. S., Sanderfoot A. A., Ye C. M., Silva M. A. T., et al. (2009). Analysis of potato virus X replicase and TGBp3 subcellular locations. Virology 393 272–285 10.1016/j.virol.2009.08.002 - DOI - PubMed

LinkOut - more resources