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JXB Advance Access originally published online on March 14, 2003
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Journal of Experimental Botany, Vol. 54, No. 386, pp. 1335-1341, May 1, 2003
© 2003 Oxford University Press

A germin-like protein of wheat leaf apoplast inhibits serine proteases

Received 15 October 2002; Accepted 24 January 2003

Carmen Inés Segarra3,1,2, Claudia Anahí Casalongué1,2, Marcela Lilian Pinedo1, Virginia Paola Ronchi1 and Rubén Danilo Conde1

1 Instituto de Investigaciones Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CC 1245, B7600GTQ, Mar del Plata, Argentina
2 Departamento de Biología, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CC 1245, B7600GTQ, Mar del Plata, Argentina

3 To whom correspondence should be addressed. E-mail: segarra{at}mdp.edu.ar

A protein resistant to heat and proteolysis that inhibits serine proteases was isolated from wheat leaf apoplasts. Based on trypsin inhibition, its more active form was a 66–69 kDa oligomer. It was dissociated in an 18–21 kDa monomer having an amino terminal sequence identical to the Box A of germins and germin-like proteins. Like these proteins, it was glycosylated and showed manganese superoxide dismutase activity. The monomer displayed three forms when examined by 2D western blot: two of 19 kDa, pI 5.8 and 6.2; and one of 21 kDa, pI 5.8. It was found that the protein controls serine protease activity in the apoplast of plants challenged with the fungus Septoria tritici.

Key words: Apoplast, germin, serine protease inhibitor, wheat leaf.


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