Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features

• DOI: 10.1002/prot.20405
• Publication Date: 2005-02-22T21:47:34Z
• Authors: Pedro Da Silva; Céline Landon; Benoit Industri; Antoine Marais; Didier Marion; Michel Ponchet; Françoise Vovelle
• Keywords: Intrinsically Disordered Proteins

Plant lipid transfer proteins are small soluble extracellular that able to bind and a variety of lipids in vitro. Recently, it has been proposed may play key role plant defence mechanisms, especially during the induction systemic acquired resistance. However, very little is known about expressed developing plants tissues, since almost all biophysical structural data available date on originate from present storage tissues monocot cereal seeds. In this paper, we report functional characteristics protein (named LTP1_1) constitutively young aerial organs Nicotiana tabacum (common tobacco). The unlabelled uniformly labelled were produced yeast Pichia pastoris, determined three-dimensional (3D) structure LTP1_1 using nuclear magnetic resonance (NMR) spectroscopy molecular modeling techniques. global fold close previously published structures LTP1 extracted seeds, including an internal cavity. chemical shift variations several NMR signals upon binding show tobacco only one LysoMyristoylPhosphatidylCholine (LMPC), while wheat maize LTPs can either or two. Titration experiments intrinsic tyrosine fluorescence confirm result not with LMPC but also two fatty acids. These differences be explained by presence hydrophobic cluster closing second possible access This suggests properties could modulated subtle changes conserved structure. biological significance finding discussed light signalling LTP1_1-jasmonate complex described elsewhere.