Processing of Thionin Precursors in Barley Leaves by a Vacuolar Proteinase

Romero, Alicia and Alamillo, Josefa M. and García Olmedo, Francisco (1997). Processing of Thionin Precursors in Barley Leaves by a Vacuolar Proteinase. "The FEBS Journal. European Journal of Biochemistry", v. 243 (n. 1-2); pp. 202-208. ISSN 1742-4658. https://doi.org/10.1111/j.1432-1033.1997.0202a.x.

Description

Title: Processing of Thionin Precursors in Barley Leaves by a Vacuolar Proteinase
Author/s:
  • Romero, Alicia
  • Alamillo, Josefa M.
  • García Olmedo, Francisco
Item Type: Article
Título de Revista/Publicación: The FEBS Journal. European Journal of Biochemistry
Date: January 1997
Volume: 243
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Thionins are synthesized as precursors with a signal peptide and a long C-terminal acidic peptide that is post-translationally processed. A fusion protein including the maltose-binding protein from Eschrrichia coli (MalE), thionin DG3 froin barley leaves, and its acidic C-terminal peptide has been used to obtain antibodies that recognize both domains of the precursor. In barley leaf sections. mature thionins accuinulated in the vacuolar content, while the acidic peptide was not detected in any cell fraction. Brefeldin A and inonensin inhibited processing of the precursor but its export from the microsomal fraction was not inhibited. Both purified vacuoles aiid an acid (pH 5.5) extract from leaves processed the fusion protein into a MalE-thionin and an acidic peptide fragment. A 70-kDa proteinase that effected this cleavage was purified froin the acid extract. Processing of the fusion protein by both lysed vacuoles and the purified proteinase was inhibited by Zn2+ and by Cu2+, but not by inhibitors of the previously described vacuolar processing thiol or aspartic proteinases. In vivo processing of the thionin precursor in leaf sections was also inhibited by Zn+, and Cu2+, Variants of the fusion protein with altered processing sites that represented thme of thionin precursors from different taxa were readily processed by the proteinase, whereas changing the polarity of either the C-terminal or N-terminal residues of the processing site prevented cleavage by the proteinase.

More information

Item ID: 5853
DC Identifier: http://oa.upm.es/5853/
OAI Identifier: oai:oa.upm.es:5853
DOI: 10.1111/j.1432-1033.1997.0202a.x
Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1997.0202a.x/full
Deposited by: Memoria Investigacion
Deposited on: 02 Feb 2011 09:23
Last Modified: 20 Apr 2016 14:33
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