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Journal of Virology, May 2004, p. 4817-4826, Vol. 78, No. 9
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.9.4817-4826.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

A Novel Motif in Geminivirus Replication Proteins Interacts with the Plant Retinoblastoma-Related Protein

Gerardo Arguello-Astorga,{dagger} Luisa Lopez-Ochoa, Ling-Jie Kong,{ddagger} Beverly M. Orozco,§ Sharon B. Settlage, and Linda Hanley-Bowdoin*

Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695-7622

Received 22 October 2003/ Accepted 9 December 2003

The geminivirus replication factor AL1 interacts with the plant retinoblastoma-related protein (pRBR) to modulate host gene expression. The AL1 protein of tomato golden mosaic virus (TGMV) binds to pRBR through an 80-amino-acid region that contains two highly predicted {alpha}-helices designated 3 and 4. Earlier studies suggested that the helix 4 motif, whose amino acid sequence is strongly conserved across geminivirus replication proteins, plays a role in pRBR binding. We generated a series of alanine substitutions across helix 4 of TGMV AL1 and examined their impact on pRBR binding using yeast two-hybrid assays. These experiments showed that several helix 4 residues are essential for efficient pRBR binding, with a critical residue being a leucine at position 148 in the middle of the motif. Various amino acid substitutions at leucine-148 indicated that both structural and side chain components contribute to pRBR binding. The replication proteins of the geminiviruses tomato yellow leaf curl virus and cabbage leaf curl virus (CaLCuV) also bound to pRBR in yeast dihybrid assays. Mutation of the leucine residue in helix 4 of CaLCuV AL1 reduced binding. Together, these results suggest that helix 4 and the conserved leucine residue are part of a pRBR-binding interface in begomovirus replication proteins.

* Corresponding author. Mailing address: North Carolina State University, Department of Molecular and Structural Biochemistry, 128 Polk Hall, Box 7622, Raleigh, NC 27695. Phone: (919) 515-6663. Fax: (919) 515-2047. E-mail: linda_hanley-bowdoin{at}ncsu.edu.

{dagger} Present address: Departamento de Biología Molecular, Instituto de Potosino de Investigaciones Científicas y Tecnológicas, 78216 San Luis Potosí, SLP, México.

{ddagger} Present address: Department of Genetics, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710.

§ Present address: Bayer Corporation, Clayton, NC 27520.

Journal of Virology, May 2004, p. 4817-4826, Vol. 78, No. 9
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.9.4817-4826.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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