Proceedings of the XLVI Italian Society of Agricultural Genetics - SIGA Annual Congress

Giardini Naxos, Italy - 18/21 September, 2002

ISBN 88-900622-3-1

Poster Abstract - 5.12

MOLECULAR CLONING OF A TRYPSIN INHIBITOR CDNA FROM SNAIL MEDIC (MEDICAGO SCUTELLATA) SEEDS

BALESTRAZZI A.*, CONFALONIERI M.**, TAVA A.**, ODOARDI M.**, CARBONERA D.*

*)Dipartimento di Genetica e Microbiologia “A. Buzzati-Traverso”, Università di Pavia

**) Istituto Sperimentale Colture Foraggere - MiPAF, Lodi

Medicago scutellata, proteinase inhibitors

Proteinase inhibitors from plants have been intensively investigated in order to define their chemical structure and biological function. They act as defence proteins in plants against pathogen attack, regulators of endogenous protease activity and as storage proteins. In a previous study the expression pattern of MsTI gene from Medicago scutellata, an annual pasture legume, has been evaluated by northern blot analysis, using an heterologous probe from Medicago sativa. Following exposure to several biotic and abiotic stresses, both local and systemic accumulation of MsTI mRNA was observed. Moreover, the presence of a multigene family has been demonstrated. We have recently isolated a small (180 bp) cDNA fragment, encoding the MsTI protein. The MsTI cDNA was obtained by RT-PCR performend on poly(A)+ mRNA purified from immature seeds using degenerated oligonucleotides. The nucleotide sequence showed an homology of 75% compared with the corresponding sequence of the ATI inhibitor from M. sativa. Isolation of both 5’ and 3’ cDNA ends of the MsTI cDNA will be performed using a RACE-based approach. The availability of the full-lenght MsTI cDNA will allow performing structural studies on the corresponding recombinant protein as well as production of transgenic plants for insect pest resistance. Identification and functional characterization of the wound-inducible MsTI promoter will be also relevant for biotechnological applications.