The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Schmid, M., Simpson, D. J., Sarioglu, H., Lottspeich, F., & Gietl, C. Proceedings of the National Academy of Sciences, 98(9):5353–5358, April, 2001. Publisher: National Academy of Sciences Section: Biological Sciences![The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The ricinosome (synonym, precursor protease vesicle) is a novel organelle, found so far exclusively in plant cells. Electron microscopic studies suggest that it buds off from the endoplasmic reticulum in senescing tissues. Biochemical support for this unusual origin now comes from the composition of the purified organelle, which contains large amounts of a 45-kDa cysteine endoprotease precursor with a C-terminal KDEL motif and the endoplasmic reticulum lumen residents BiP (binding protein) and protein disulfide isomerase. Western blot analysis, peptide sequencing, and mass spectrometry demonstrate retention of KDEL in the protease proform. Acidification of isolated ricinosomes causes castor bean cysteine endopeptidase activation, with cleavage of the N-terminal propeptide and the C-terminal KDEL motif. We propose that ricinosomes accumulate during senescence by programmed cell death and are activated by release of protons from acidic vacuoles.
@article{schmid_ricinosomes_2001,
title = {The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum},
volume = {98},
copyright = {Copyright © 2001, The National Academy of Sciences},
issn = {0027-8424, 1091-6490},
url = {https://www.pnas.org/content/98/9/5353},
doi = {10.1073/pnas.061038298},
abstract = {The ricinosome (synonym, precursor protease vesicle) is a novel organelle, found so far exclusively in plant cells. Electron microscopic studies suggest that it buds off from the endoplasmic reticulum in senescing tissues. Biochemical support for this unusual origin now comes from the composition of the purified organelle, which contains large amounts of a 45-kDa cysteine endoprotease precursor with a C-terminal KDEL motif and the endoplasmic reticulum lumen residents BiP (binding protein) and protein disulfide isomerase. Western blot analysis, peptide sequencing, and mass spectrometry demonstrate retention of KDEL in the protease proform. Acidification of isolated ricinosomes causes castor bean cysteine endopeptidase activation, with cleavage of the N-terminal propeptide and the C-terminal KDEL motif. We propose that ricinosomes accumulate during senescence by programmed cell death and are activated by release of protons from acidic vacuoles.},
language = {en},
number = {9},
urldate = {2021-11-02},
journal = {Proceedings of the National Academy of Sciences},
author = {Schmid, Markus and Simpson, David J. and Sarioglu, Hakan and Lottspeich, Friedrich and Gietl, Christine},
month = apr,
year = {2001},
pmid = {11296243},
note = {Publisher: National Academy of Sciences
Section: Biological Sciences},
keywords = {Ricinus communis, papain-type KDEL peptidase},
pages = {5353--5358},
}
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