Journal Article

Isolation of a Putative Receptor for KDEL-tailed Cysteine Proteinase (SH-EP) from Cotyledons of <i>Vigna mungo</i> Seedlings

Akiko Tsuru-Furuno, Takashi Okamoto and Takao Minamikawa

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 42, issue 10, pages 1062-1070
Published in print October 2001 | ISSN: 0032-0781
Published online October 2001 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pce134
Isolation of a Putative Receptor for KDEL-tailed Cysteine Proteinase (SH-EP) from Cotyledons of Vigna mungo Seedlings

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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SH-EP is the major papain-type proteinase expressed in cotyledons of germinated Vigna mungo seeds. The proteinase possesses a KDEL sequence at the C-terminus although the mature form of SH-EP is localized in vacuoles. It has also been shown that the proform of SH-EP is accumulated at the edge or middle region of the endoplasmic reticulum, and the accumulated proSH-EP is directly transported to vacuoles via the KDEL-tailed cysteine proteinase-accumulating vesicle, KV. In this study, to address the transport machinery of proSH-EP through KV, putative receptor for proSH-EP was isolated from membrane proteins of cotyledons of V. mungo seedlings using a proSH-EP-immobilized column. The deduced amino acid sequence from cDNA to the protein revealed that the putative receptor for proSH-EP is a member of vacuolar sorting receptor, VSR, that is known to be localized in the Golgi-complex and/or clathrin coated vesicle. We carried out subcellular fractionation of cotyledon cells and subsequently conducted SDS-PAGE/immunoblotting and immunocytochemistry with anti-V. mungo VSR (VmVSR) or SH-EP antibody. The results showed that VmVSR is co-localized in the fraction of the gradient in which KV existed.

Keywords: Key words: Cysteine proteinase — KDEL sequence — Protein transport — Receptor — Vacuole.; The nucleotide sequence reported in this paper has been submitted to DDBJ under accession number AB056693.

Journal Article.  6352 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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