tailieunhanh - Báo cáo khoa học: Calmodulin binds to maize lipid transfer protein and modulates its lipids binding ability

Tham khảo luận văn - đề án 'báo cáo khoa học: calmodulin binds to maize lipid transfer protein and modulates its lipids binding ability', luận văn - báo cáo, báo cáo khoa học phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | ễFEBS Journal Calmodulin binds to maize lipid transfer protein and modulates its lipids binding ability Cuifeng Li Wanqin Xie Wenyan Bai Zhenpeng Li Yulong Zhao and Hua Liuf Department of Biochemistry and Molecular Biology Nankai University Tianjin China Keywords calcium-independent mode calmodulin-binding domain CaMBP-10 lipid transfer protein lipid-binding activity Correspondence C. Li Department of Biochemistry and Molecular Biology Nankai University Tianjin 300071 China Fax 86 22 2350 8800 Tel 86 22 2350 3585 E-mail licf@ These authors contributed equally to this work FPresent address Department of Pharmacology and Molecular Sciences Johns Hopkins University Baltimore MD USA Received 15 June 2008 revised 24 August 2008 accepted 27 August 2008 doi Although plant non-specific lipid transfer proteins ns-LTPs are characterized by their ability to bind and transfer a broad range of hydrophobic ligands in vitro their biological functions in vivo remain unclear. Recently it has been proposed that ns-LTPs may play a key role in plant defense mechanisms particularly during the induction of systemic acquired resistance however very little is known about the regulation in this process. We report that the binding of maize non-specific lipid transfer protein Zm-LTP to calmodulin CaM is in a calcium-independent manner. To better understand the interaction mechanism between Zm-LTP and CaM the CaM-binding site of Zm-LTP was mapped to the region of amino acids 46-60. Point mutations indicate that four amino acid residues R46 R47 K54 and R58 in this region are crucial for binding. Furthermore we tested the effects of CaM on the lipid-binding activity of Zm-LTP in the presence of Ca2 EGTA N- 6-aminohexyl -5-chloro-1-naphthalene sulfonamide and trifluoperazine respectively. We also investigated the structural features of CaM-binding motifs in LTPs from different species and strong differences were observed. Taken together our results .

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