Abstract
The DNA-binding activity and DNA-binding domain of Tomato yellow leaf curl Thailand virus coat protein were investigated. A full-length coat protein (CP) and two truncated derivatives lacking the amino (CPΔ1-62) and carboxyl (CPΔ126-257) termini were produced in Escherichia coli as fusion proteins to glutathione-S-transferase (GST). Southwestern analysis showed that GST-CP bound both single-stranded (ss) and double-stranded (ds) DNA, while GST-CPΔ126-257 interacted only with ssDNA. Neither ss nor dsDNA bound to GST-CPΔ1-62. The results suggested that a putative DNA-binding domain is located at the N-terminal 1-62 amino residues.
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The nucleotide sequence data reported are available in the DDBJ/EMBL/GenBank databases under accession numbers AF141922 (TYLCTHV-[2]), AF220561 (RTBVCN), X01633 (MSV) and AF295401 (ToLCBV-[Ban5])
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Pitaksutheepong, C., Vimoltat, A., Nathwong, B. et al. The N-terminal 62 amino acid residues of the coat protein of Tomato yellow leaf curl Thailand virus are responsible for DNA binding. J Gen Plant Pathol 73, 72–75 (2007). https://doi.org/10.1007/s10327-006-0317-5
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DOI: https://doi.org/10.1007/s10327-006-0317-5