A novel lipid transfer protein from the dill Anethum graveolens L.: isolation, structure, heterologous expression, and functional characteristics.

Melnikova, Daria N; Mineev, Konstantin S; Finkina, Ekaterina I; Arseniev, Alexander S; Ovchinnikova, Tatiana V

Melnikova, Daria N; Mineev, Konstantin S; Finkina, Ekaterina I; Arseniev, Alexander S; Ovchinnikova, Tatiana V.

Afiliación

Melnikova DN; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.
Mineev KS; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.
Finkina EI; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.
Arseniev AS; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.
Ovchinnikova TV; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.

J Pept Sci ; 22(1): 59-66, 2016 Jan.

Article en En | MEDLINE | ID: mdl-26680443

RESUMEN

A novel lipid transfer protein, designated as Ag-LTP, was isolated from aerial parts of the dill Anethum graveolens L. Structural, antimicrobial, and lipid binding properties of the protein were studied. Complete amino acid sequence of Ag-LTP was determined. The protein has molecular mass of 9524.4 Da, consists of 93 amino acid residues including eight cysteines forming four disulfide bonds. The recombinant Ag-LTP was overexpressed in Escherichia coli and purified. NMR investigation shows that the Ag-LTP spatial structure contains four α-helices, forming the internal hydrophobic cavity, and a long C-terminal tail. The measured volume of the Ag-LTP hydrophobic cavity is equal to ~800 A(3), which is much larger than those of other plant LTP1s. Ag-LTP has weak antifungal activity and unpronounced lipid binding specificity but effectively binds plant hormone jasmonic acid. Our results afford further molecular insight into biological functions of LTP in plants.

Asunto(s)

Anethum graveolens/química; Proteínas Portadoras/química; Proteínas de Plantas/química; Secuencia de Aminoácidos; Anethum graveolens/metabolismo; Proteínas Portadoras/genética; Proteínas Portadoras/metabolismo; Clonación Molecular; Ciclopentanos/química; Escherichia coli/genética; Escherichia coli/metabolismo; Expresión Génica; Interacciones Hidrofóbicas e Hidrofílicas; Modelos Moleculares; Datos de Secuencia Molecular; Peso Molecular; Oxilipinas/química; Componentes Aéreos de las Plantas/química; Proteínas de Plantas/genética; Proteínas de Plantas/metabolismo; Unión Proteica; Estructura Secundaria de Proteína; Estructura Terciaria de Proteína; Proteínas Recombinantes/química; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Alineación de Secuencia

Palabras clave

Anethum graveolens L; NMR; antimicrobial activity; dill; lipid binding; lipid transfer protein; recombinant expression; spatial structure

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Proteínas Portadoras / Anethum graveolens Tipo de estudio: Prognostic_studies Idioma: En Revista: J Pept Sci Asunto de la revista: BIOQUIMICA Año: 2016 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Reino Unido

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