Purification and Primary Structure of Novel Lipid Transfer Proteins from Germinated Lentil (Lens culinaris) Seeds

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E. I. Finkina¹, S. V. Balandin¹, M. V. Serebryakova², N. A. Potapenko¹, A. A. Tagaev¹, and T. V. Ovchinnikova^1*

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (495) 336-4333; E-mail: ovch@ibch.ru

²Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, ul. Pogodinskaya 10, 119121 Moscow, Russia; fax: (495) 245-0857

^* To whom correspondence should be addressed.

Received November 23, 2006; Revision received December 18, 2006

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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.

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KEY WORDS: lipid transfer proteins, lentil, germinated seeds, primary structure, antibacterial activity, cDNA

DOI: 10.1134/S0006297907040104

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