Journal Article

PreJuSER-9618

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png LeSBT1, a subtilase from tomato plants

Janzik, I.FZJ* ; Macheroux, P. ; Amrhein, N. ; Schaller, A.

2000
Soc. Bethesda, Md.

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Please use a persistent id in citations: http://hdl.handle.net/2128/2841

Abstract: The cDNA of a tomato subtilase designated LeSBT1 was cloned from a tomato flower cDNA library. The deduced amino acid sequence indicated for LeSBT1 the structure of a prepro-protein targeted to the secretory pathway by virtue of an amino-terminal signal peptide. LeSBT1 was expressed in the baculovirus/insect cell system and a processed 73-kDa form of LeSBT1, lacking both signal peptide and prodomain, was purified to homogeneity from culture supernatants, This 73-kDa LeSBT1, however, lacked proteolytic activity. Zymogen activation to yield 68-kDa LeSBT1 required the additional processing of an amino-terminal autoinhibitory peptide in a strictly pH-dependent manner. Mature 68-kDa LeSBT1 showed highest activity at acidic pH consistent with its presumed localization in the apoplast of the plant cell. In comparison to other plant subtilases, LeSBT1 exhibited a narrower substrate specificity in that it cleaves only polypeptide substrates preferentially but not exclusively carboxyl-terminal of glutamine residues. The possible involvement of LeSBT1 in selective proprotein processing is discussed with reference to the related mammalian proprotein convertases.

Keyword(s): J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologie des Stoffaustauschs (ICG-6)

Research Program(s):

1. Pflanzenphysiologie des Spurengasaustauschs mit der Atmosphäre (36.61.0)

Appears in the scientific report 2000

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Database coverage:

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