Purification and primary structure of novel lipid transfer proteins from germinated lentil (Lens culinaris) seeds

被引:23
作者
Finkina, E. I.
Balandin, S. V.
Serebryakova, M. V.
Potapenko, N. A.
Tagaev, A. A.
Ovchinnikova, T. V.
机构
[1] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
[2] Russian Acad Med Sci, Orekhovich Inst Biomed Chem, Moscow 119121, Russia
关键词
lipid transfer proteins; lentil; germinated seeds; primary structure; antibacterial activity; cDNA;
D O I
10.1134/S0006297907040104
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A subfamily of eight novel lipid transfer proteins designated as Lc-LTP1-8 was found in the lentil Lens culinaris. Lc-LTP2, Lc-LTP4, Lc-LTP7, and Lc-LTP8 were purified from germinated lentil seeds, and their molecular masses (9268.7, 9282.7, 9121.5, 9135.5 daltons) and complete amino acid sequences were determined. The purified proteins consist of 92-93 amino acid residues, have four disulfide bonds, and inhibit growth of Agrobacterium tumefaciens. Total RNA was isolated from germinated lentil seeds, RT-PCR and cloning were performed, and the cDNAs of six LTPs were sequenced. Precursor 116-118-residue proteins with 24-25-residue signal peptides were found, and two of them are purified proteins Lc-LTP2 and Lc-LTP4.
引用
收藏
页码:430 / 438
页数:9
相关论文
共 35 条
[1]  
[Anonymous], 1989, Molecular Cloning
[2]   Component-resolved in vitro diagnosis in carrot allergy:: Does the use of recombinant carrot allergens improve the reliability of the diagnostic procedure? [J].
Ballmer-Weber, BK ;
Wangorsch, A ;
Bohle, B ;
Kaul, S ;
Kündig, T ;
Fötisch, K ;
van Ree, R ;
Vieths, S .
CLINICAL AND EXPERIMENTAL ALLERGY, 2005, 35 (07) :970-978
[3]   From elicitins to lipid-transfer proteins:: a new insight in cell signalling involved in plant defence mechanisms [J].
Blein, JP ;
Coutos-Thévenot, P ;
Marion, D ;
Ponchet, M .
TRENDS IN PLANT SCIENCE, 2002, 7 (07) :293-296
[4]  
Castro MS, 2005, PROTEIN PEPTIDE LETT, V12, P13
[5]   Pro-apoptotic effect of maize lipid transfer protein on mammalian mitochondria [J].
Crimi, M ;
Astegno, A ;
Zoccatelli, G ;
Esposti, MD .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2006, 445 (01) :65-71
[6]   Changes in the tobacco leaf apoplast proteome in response to salt stress [J].
Dani, V ;
Simon, WJ ;
Duranti, M ;
Croy, RRD .
PROTEOMICS, 2005, 5 (03) :737-745
[7]   Recombinant Pru p 3 and natural Pru p 3, a major peach allergen, show equivalent immunologic reactivity:: A new tool for the diagnosis of fruit allergy [J].
Díaz-Perales, A ;
Sanz, ML ;
García-Casado, G ;
Sánchez-Monge, R ;
García-Selles, FJ ;
Lombardero, M ;
Polo, F ;
Gamboa, PM ;
Barber, D ;
Salcedo, G .
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 2003, 111 (03) :628-633
[8]   Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1) [J].
Douliez, JP ;
Michon, T ;
Marion, D .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2000, 1467 (01) :65-72
[9]   Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2 [J].
Douliez, JP ;
Pato, C ;
Rabesona, H ;
Mollé, D ;
Marion, D .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (05) :1400-1403
[10]   Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels [J].
Douliez, JP ;
Michon, T ;
Elmorjani, K ;
Marion, D .
JOURNAL OF CEREAL SCIENCE, 2000, 32 (01) :1-20