A unique mechanism for protein processing and degradation in Arabidopsis thaliana

被引：122

作者：

Rojo, E

Zouhar, J

Carter, C

Kovaleva, V

Raikhel, NV ^{[1
]}

机构：

[1] Univ Calif Riverside, Dept Bot & Plant Sci, Riverside, CA 92521 USA

[2] Univ Calif Riverside, Ctr Plant Cell Biol, Riverside, CA 92521 USA

[3] CSIC, Ctr Nacl Biotecnol, Dept Genet Mol Plantas, E-28049 Madrid, Spain

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 12期

关键词：

D O I：

10.1073/pnas.1230987100

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：7389 / 7394

页数：6

共 21 条

[1] The plant vacuolar sorting receptor AtELP is involved in transport of NH2-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana [J].