Abstract:
:Nonspecific lipid transfer protein (nsLTP) is usually basic and secreted low-molecular-mass protein in plants. The 3-D structure of nsLTP1 resembles that of elicitin produced by the plant pathogen Phytophthora cryptogea, which can bind to the plant plasma membrane putative receptor and activate the downstream responses. It is inferred that nsLTP1 may have similar binding sites on the plasma membranes. In this work, rice recombinant protein TRX-nsLTP110 labeled with (125)I was shown to bind to rice plasma membrane preparations in a saturable curve, with an apparent K(d) of 13.6 nM and B(max) of 150 fmol/mg proteins. Competition experiments revealed that the binding of TRX-nsLTP110 was specific, in contrast to the nonspecific binding of the fusion tag thioredoxin. Protease treatment assay showed that the binding sites were proteinaceous. Our results suggest that the binding sites of nsLTPs on plasma membranes may be ubiquitous in the plant kingdom. They may be competed out from the binding sites under pathogen attack, supporting a role for nsLTP1 in host defense response to pathogens.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Wang X,Wang H,Li Y,Cao K,Ge Xdoi
10.1007/s11033-008-9238-zsubject
Has Abstractpub_date
2009-04-01 00:00:00pages
745-50issue
4eissn
0301-4851issn
1573-4978journal_volume
36pub_type
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