Previous Article | Next Article 
Journal of Virology, March 2000, p. 2067-2072, Vol. 74, No. 5
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Interaction of the Cauliflower Mosaic Virus Coat
Protein with the Pregenomic RNA Leader
Orlene
Guerra-Peraza,
Marc
de Tapia,
Thomas
Hohn,* and
Maja
Hemmings-Mieszczak
Friedrich Miescher-Institut, CH-4002 Basel,
Switzerland
Received 18 June 1999/Accepted 2 December 1999
Using the yeast three-hybrid system, the interaction of the
Cauliflower mosaic virus (CaMV) pregenomic 35S RNA (pgRNA)
leader with the viral coat protein, its precursor, and a series of
derivatives was studied. The purine-rich domain in the center of the
pgRNA leader was found to specifically interact with the coat protein. The zinc finger motif of the coat protein and the preceding basic domain were essential for this interaction. Removal of the N-terminal portion of the basic domain led to loss of specificity but did not
affect the strength of the interaction. Mutations of the zinc finger
motif abolished not only the interaction with the RNA but also viral
infectivity. In the presence of the very acidic C-terminal domain,
which is part of the preprotein but is not present in the mature CP,
the interaction with the RNA was undetectable.
*
Corresponding author. Mailing address: Friedrich
Miescher-Institut, Maulbeerstrasse 66, 4058 Basel, Switzerland. Phone:
(061) 6976672. Fax: (061) 6973976. E-mail: hohn{at}fmi.ch.

Permanent address: Centro de Bioplanta, Ciego de Avila,
Cuba.

Present address: IPCB-UMR 7519, 67084 Strasbourg,
France.
Journal of Virology, March 2000, p. 2067-2072, Vol. 74, No. 5
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Schepetilnikov, M., Schott, G., Katsarou, K., Thiebeauld, O., Keller, M., Ryabova, L. A.
(2009). Molecular dissection of the prototype foamy virus (PFV) RNA 5'-UTR identifies essential elements of a ribosomal shunt. Nucleic Acids Res
37: 5838-5847
[Abstract]
[Full Text]
-
Chapdelaine, Y., Kirk, D., Karsies, A., Hohn, T., Leclerc, D.
(2002). Mutation of Capsid Protein Phosphorylation Sites Abolishes Cauliflower Mosaic Virus Infectivity. J. Virol.
76: 11748-11752
[Abstract]
[Full Text]
-
Kobayashi, K., Tsuge, S., Stavolone, L., Hohn, T.
(2002). The Cauliflower Mosaic Virus Virion-Associated Protein Is Dispensable for Viral Replication in Single Cells. J. Virol.
76: 9457-9464
[Abstract]
[Full Text]
-
Karsies, A., Merkle, T., Szurek, B., Bonas, U., Hohn, T., Leclerc, D.
(2002). Regulated nuclear targeting of cauliflower mosaic virus. J. Gen. Virol.
83: 1783-1790
[Abstract]
[Full Text]
-
Takemoto, Y., Hibi, T.
(2001). Genes Ia, II, III, IV and V of Soybean chlorotic mottle virus are essential but the gene Ib product is non-essential for systemic infection. J. Gen. Virol.
82: 1481-1489
[Abstract]
[Full Text]
-
Pooggin, M. M., Futterer, J., Skryabin, K. G., Hohn, T.
(2001). Ribosome shunt is essential for infectivity of cauliflower mosaic virus. Proc. Natl. Acad. Sci. USA
98: 886-891
[Abstract]
[Full Text]
-
HOHN, T., PARK, H.-S., GUERRA-PERAZA, O., STAVOLONE, L., POOGGIN, M.M., KOBAYASHI, K., RYABOVA, L.A.
(2001). Shunting and Controlled Reinitiation: The Encounter of Cauliflower Mosaic Virus with the Translational Machinery. Cold Spring Harb Symp Quant Biol
66: 269-276
[Abstract]
-
Hemmings-Mieszczak, M., Hohn, T., Preiss, T.
(2000). Termination and Peptide Release at the Upstream Open Reading Frame Are Required for Downstream Translation on Synthetic Shunt-Competent mRNA Leaders. Mol. Cell. Biol.
20: 6212-6223
[Abstract]
[Full Text]
-
Herzog, E., Guerra-Peraza, O., Hohn, T.
(2000). The Rice Tungro Bacilliform Virus Gene II Product Interacts with the Coat Protein Domain of the Viral Gene III Polyprotein. J. Virol.
74: 2073-2083
[Abstract]
[Full Text]
-
Ryabova, L. A., Pooggin, M. M., Dominguez, D. I., Hohn, T.
(2000). Continuous and Discontinuous Ribosome Scanning on the Cauliflower Mosaic Virus 35 S RNA Leader Is Controlled by Short Open Reading Frames. J. Biol. Chem.
275: 37278-37284
[Abstract]
[Full Text]