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Abstract
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Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni.

I Hara-Nishimura, Y Takeuchi, M Nishimura
I Hara-Nishimura
Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.
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Y Takeuchi
Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.
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M Nishimura
Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.
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Published November 1993. DOI: https://doi.org/10.1105/tpc.5.11.1651

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  • Copyright © 1993 by American Society of Plant Biologists

Abstract

Proproteins of various vacuolar proteins are post-translationally processed into mature forms by the action of a unique vacuolar processing enzyme. If such a processing enzyme is transported to vacuoles together with proprotein substrates, the enzyme must be a latent form. Immunocytochemical localization of a vacuolar processing enzyme, a 37-kD cysteine proteinase, in the endosperm of maturing castor bean seeds places the enzyme in the vacuolar matrix, where a variety of proproteins is also present. To characterize a molecular structure of vacuolar processing enzyme, we isolated a cDNA for the enzyme. Deduced primary structure of a 55-kD precursor is 33% identical to a putative cysteine proteinase of the human parasite Schistosoma mansoni. The precursor is composed of a signal peptide, a 37-kD active processing enzyme domain, and a propeptide fragment. Although the precursor expressed in Escherichia coli has no vacuolar processing activity, a 36-kD immunopositive protein expressed in E. coli is active. These results suggest that the activation of the vacuolar processing enzyme requires proteolytic cleavage of a 14-kD C-terminal propeptide fragment of the precursor.

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Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni.
I Hara-Nishimura, Y Takeuchi, M Nishimura
The Plant Cell Nov 1993, 5 (11) 1651-1659; DOI: 10.1105/tpc.5.11.1651

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Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni.
I Hara-Nishimura, Y Takeuchi, M Nishimura
The Plant Cell Nov 1993, 5 (11) 1651-1659; DOI: 10.1105/tpc.5.11.1651
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Vol. 5, Issue 11
Nov 1993
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