Home LiteratureArticle Details

PMID: 12773619 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

A unique mechanism for protein processing and degradation in Arabidopsis thaliana.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 100 ·No. 12 ·2003-06-10 ·Pages 7389-94

Rojo E, Zouhar J, Carter C, Kovaleva V, Raikhel NV

Abstract

Precursor protease vesicles are plant-specific compartments containing precursors of enzymes that are thought to participate in the degradation of cellular components in organs undergoing senescence. We report in vivo evidence that the precursor protease vesicle-localized vacuolar processing enzyme-gamma (VPEgamma) is critical for maturation of the plant vacuolar protease AtCPY. We also provide biochemical and functional evidence that VPEgamma is involved in degradation of the vacuolar invertase AtFruct4 in aging tissues. Moreover, a proteomics-based approach identified various proteins found in the vacuoles of aging vpegamma mutants but not in WT plants, suggesting a unique role of VPEgamma in protein processing and degradation in Arabidopsis.

MeSH Terms

Arabidopsis/genetics,metabolism Arabidopsis Proteins/genetics,metabolism Carboxypeptidases/metabolism Cathepsin A Cysteine Endopeptidases/genetics,metabolism Genes, Plant Glycoside Hydrolases/metabolism Microscopy, Immunoelectron Mutagenesis, Insertional Mutation Protein Processing, Post-Translational Vacuoles/metabolism beta-Fructofuranosidase

Chemicals

Arabidopsis Proteins Glycoside Hydrolases beta-Fructofuranosidase Carboxypeptidases Cathepsin A Cysteine Endopeptidases vacuolar processing enzyme gamma, Arabidopsis

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Rojo Enrique

Department of Botany and Plant Sciences and Center for Plant Cell Biology, University of California, Riverside, CA 92521, USA.

Zouhar Jan

Carter Clay

Kovaleva Valentina

Raikhel Natasha V

References (20)

20 references, click to expand

T-DNA as an insertional mutagen in Arabidopsis.
Plant Cell. 1999 Dec;11(12):2283-90 PMID: 10590158
Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions.
Plant J. 1999 Jul;19(1):43-53 PMID: 10417725
An acyltransferase catalyzing the formation of diacylglucose is a serine carboxypeptidase-like protein.
Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6902-7 PMID: 10829071
The plant vacuolar sorting receptor AtELP is involved in transport of NH(2)-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana.
J Cell Biol. 2000 Jun 26;149(7):1335-44 PMID: 10871276
Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles.
Plant Physiol. 2000 Aug;123(4):1227-34 PMID: 10938342
A maize vacuolar invertase, IVR2, is induced by water stress. Organ/tissue specificity and diurnal modulation of expression.
Plant Physiol. 2000 Sep;124(1):71-84 PMID: 10982423
The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum.
Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5353-8 PMID: 11296243
A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis.
Plant Cell Physiol. 2001 Sep;42(9):894-9 PMID: 11577182
VACUOLELESS1 is an essential gene required for vacuole formation and morphogenesis in Arabidopsis.
Dev Cell. 2001 Aug;1(2):303-10 PMID: 11702788
A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves.
Plant Physiol. 2001 Dec;127(4):1626-34 PMID: 11743107
Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide.
Plant Cell Physiol. 2002 Feb;43(2):143-51 PMID: 11867693
A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis.
Plant J. 2003 Feb;33(3):493-502 PMID: 12581307
The AtC-VPS protein complex is localized to the tonoplast and the prevacuolar compartment in arabidopsis.
Mol Biol Cell. 2003 Feb;14(2):361-9 PMID: 12589039
Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni.
Plant Cell. 1993 Nov;5(11):1651-9 PMID: 8312744
The expression of serine carboxypeptidases during maturation and germination of the barley grain.
Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8209-13 PMID: 7520177
An Arabidopsis VPS45p homolog implicated in protein transport to the vacuole.
Plant Physiol. 1998 Jun;117(2):407-15 PMID: 9625693
A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9920-5 PMID: 9707576
Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme.
J Biol Chem. 1999 Jan 22;274(4):2563-70 PMID: 9891029
Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana.
Plant J. 1998 Dec;16(6):735-43 PMID: 10069079
Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds.
J Cell Biol. 2000 Feb 7;148(3):453-64 PMID: 10662772

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.1230987100

Published

2003-06-10

Epub

2003-00-28

Pages

7389-94

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC165885

Subset

External Links

PubMed source DOI: 10.1073/pnas.1230987100 PMC Full Text View journal details

Analysis Services

A unique mechanism for protein processing and degradation in Arabidopsis thaliana.

Contact

WeChat Official Account