Previous Article | Next Article ![]()
Journal of Virology, January 2003, p. 696-700, Vol. 77, No. 1
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.1.696-700.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Horticulture Research International, East Malling, West Malling, Kent ME19 6BJ,1 Centre for Biomolecular Science, University of St. Andrews, Fife KY16 9ST,2 Department of Disease and Stress Biology, John Innes Centre, Colney, Norwich NR4 7UH, United Kingdom,4 Department of Biology, East China Normal University, Shanghai 200062, China3
Received 18 July 2002/ Accepted 1 October 2002
The zinc finger C36-X1-C38-X7-C46-X6-H53 of the nuclearly localized C2 protein of Tomato yellow leaf curl virus China is involved in pathogenicity and suppression of posttranscriptional gene silencing (PTGS). Here, we demonstrate that the zinc finger is indispensable for the C2 protein to bind zinc and DNA. Mutation of cysteine residue C36, C38, or C46 reduced the zinc and DNA binding capacity of C2 protein. When expressed from potato virus X, all three mutants, C2-C36R, C2-C38N, and C2-C46I, tagged with a green fluorescent protein (GFP) were still capable of transporting GFP into but aggregated abnormally in nuclei. Our data establish that zinc- and DNA-binding activity correlates with C2-mediated pathogenesis and PTGS suppression.
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»