Protein Engineering vol. 16 no. 6 pp. 387-390, 2003
© 2003 Oxford University Press
Preliminary study on the structural basis of the antifungal activity of a rice lipid transfer protein
Department of Biochemistry and Molecular Biology, School of Life Sciences, Fudan University, Shanghai 200433, China
1 To whom correspondence should be addressed. e-mail: gexiaochun1@yahoo.com.cn
Keywords: antifungal activity/disulfide bridge/rice lipid transfer protein/site-directed mutagenesis/structure
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Introduction |
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Lipid transfer proteins (LTPs) belong to a group of proteins which occur widely in higher plants. Owing to their in vitro activity of transferring lipids between membranes, they were originally postulated to facilitate intracellular lipid transfer in vivo (Kader, 1975
, 1996). However, later evidence that they were synthesized with an N-terminal signal peptide and localized extracellularly contradicts this hypothesis (Thoma et al., 1993). Therefore, other functions were suggested, including participating in defense reactions against plant pathogen attack (Molina et al., 1993; Garcia-Olmedo et al., 1995; Maldonado et al., 2002) and transporting of cutin monomer to aid in cuticle formation (Hollenbach et al., 1997). The facts that several LTPs in maize, barley and pepper leaves were induced by pathogen infection (Molina and Garcia-Olmedo, 1993; Molina et al., 1993; Park et al., 2002), some LTP isoforms |
Materials and methods |
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Materials
Molecular modeling of LTP110
Construction of plasmids carrying mutant genes
Cloning of the sequences encoding mature proteins of wild-type and mutant LTP110 in the pET32a(+) vector
Expression and purification of thioredoxin-LTP fusion proteins
Digestion of thioredox-LTP fusion protein
Circular dichroism spectroscopy
Lipid binding assay
Inhibition test
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Results |
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Discussion |
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Acknowledgement |
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