scholarly journals Biogenesis of the Protein Storage Vacuole Crystalloid

2000 ◽  
Vol 150 (4) ◽  
pp. 755-770 ◽  
Author(s):  
Liwen Jiang ◽  
Thomas E. Phillips ◽  
Sally W. Rogers ◽  
John C. Rogers
Keyword(s):  
Seed Protein ◽  
Animal Cells ◽  
Reporter Protein ◽  
Developmentally Regulated ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Vacuolar System ◽  
Unique Mechanism ◽  
Storage Vacuole

We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage.

scholarly journals The protein storage vacuole

2001 ◽  
Vol 155 (6) ◽  
pp. 991-1002 ◽  
Author(s):  
Liwen Jiang ◽  
Thomas E. Phillips ◽  
Christopher A. Hamm ◽  
Yolanda M. Drozdowicz ◽  
Philip A. Rea ◽  
...  
Keyword(s):  
Seed Development ◽  
Secretory Pathway ◽  
Storage Proteins ◽  
Plant Seed ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Membrane Bound ◽  
Lytic Vacuole ◽  
Storage Vacuole

Storage proteins are deposited into protein storage vacuoles (PSVs) during plant seed development and maturation and stably accumulate to high levels; subsequently, during germination the storage proteins are rapidly degraded to provide nutrients for use by the embryo. Here, we show that a PSV has within it a membrane-bound compartment containing crystals of phytic acid and proteins that are characteristic of a lytic vacuole. This compound organization, a vacuole within a vacuole whereby storage functions are separated from lytic functions, has not been described previously for organelles within the secretory pathway of eukaryotic cells. The partitioning of storage and lytic functions within the same vacuole may reflect the need to keep the functions separate during seed development and maturation and yet provide a ready source of digestive enzymes to initiate degradative processes early in germination.

The Trafficking Machinery of Lytic and Protein Storage Vacuoles: How Much is Shared and How Much is Distinct?

2021 ◽  
Author(s):  
Xiuxiu Zhang ◽  
Hui Li ◽  
Hai Lu ◽  
Inhwan Hwang
Keyword(s):  
Protein Trafficking ◽  
Molecular Mechanisms ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Protein Storage Vacuole ◽  
Lytic Vacuoles ◽  
Lytic Vacuole ◽  
The Relationship ◽  
Storage Vacuole ◽  
Made In

Abstract Plant cells contain two types of vacuoles, the lytic vacuole and the protein storage vacuole. Lytic vacuoles (LVs) are present in vegetative cells, whereas protein storage vacuoles (PSVs) are found in seed cells. The physiological functions of the two vacuole types differ. Newly synthesized proteins must be transported to these vacuoles via protein trafficking through the endomembrane system for them to function. Recently, significant advances have been made in elucidating the molecular mechanisms of protein trafficking to these organelles. Despite these advances, the relationship between the trafficking mechanisms in LV and PSVs remains unclear. Some aspects of the trafficking mechanisms are common to both organelles, but certain aspects are specific to trafficking to either LV or PSVs. In this review, we summarize recent findings on the components involved in protein trafficking to both LV and PSVs and compare them to examine the extent of overlap in the trafficking mechanisms. In addition, we discuss the interconnection between the LV and PSVs in protein trafficking machinery and the implication in the identity of these organelles.

α-Galactosidase is synthesized in tomato seeds during development and is localized in the protein storage vacuoles

2001 ◽  
Vol 79 (12) ◽  
pp. 1417-1424 ◽  
Author(s):  
George W Bassel ◽  
Robert T Mullen ◽  
J Derek Bewley
Keyword(s):  
Subcellular Fractionation ◽  
Chloramphenicol Acetyltransferase ◽  
Tonoplast Intrinsic Protein ◽  
Intracellular Location ◽  
Protein Storage ◽  
Intrinsic Protein ◽  
Protein Storage Vacuoles ◽  
Tomato Seeds ◽  
Protein Storage Vacuole ◽  
Storage Vacuole

The localization of the enzyme α-galactosidase (EC 3.2.1.22) was investigated during its synthesis in developing tomato (Lycopersicon esculentum Mill.) cv. Trust seeds. This enzyme is also present in germinating seeds, where it is involved in the mobilization of carbohydrate reserves during and following seed germination. Subcellular fractionation of developing tomato seeds revealed that there is a cosedimentation between α-galactosidase activity and protein storage vacuoles in a density gradient, which is dependent upon the presence of membranes. A second approach to localizing this enzyme involved the transient transformation of protoplasts from developing tomato seeds. A reporter construct, coding for tomato α-galactosidase, fused N-terminally to the bacterial enzyme chloramphenicol acetyltransferase was used for transient expression. Immunofluorescence microscopy revealed a colocalization between the α-galactosidase - chloramphenicol acetyltransferase fusion protein and the α-tonoplast intrinsic protein, and a partial colocalization with the dark intrinsic protein (both vacuolar proteins). These data indicate that the protein storage vacuole is the intracellular location for α-galactosidase in developing tomato seeds.Key words: α-galactosidase, protein storage vacuole, seed development, seed protoplasts, tomato, tonoplast intrinsic protein.

scholarly journals Delivery of Prolamins to the Protein Storage Vacuole in Maize Aleurone Cells

2011 ◽  
Vol 23 (2) ◽  
pp. 769-784 ◽  
Author(s):  
Francisca C. Reyes ◽  
Taijoon Chung ◽  
David Holding ◽  
Rudolf Jung ◽  
Richard Vierstra ◽  
...  
Keyword(s):  
Protein Storage ◽  
Aleurone Cells ◽  
Protein Storage Vacuole ◽  
Storage Vacuole

Targeting and processing of membrane-anchored YFP fusion proteins to protein storage vacuoles in transgenic tobacco seeds

2005 ◽  
Vol 15 (4) ◽  
pp. 361-364 ◽  
Author(s):  
Ka Leung Fung ◽  
Yin Fun Yim ◽  
Yu Chung Tse ◽  
Yansong Miao ◽  
Samuel S.M. Sun ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Fusion Proteins ◽  
Seed Protein ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Protein Storage ◽  
Protein Storage Vacuoles ◽  
Pharmaceutical Proteins ◽  
Tobacco Seeds ◽  
Foreign Proteins

Seeds that store proteins in protein storage vacuoles are attractive bioreactors for producing and storing large amounts of pharmaceutical proteins. However, foreign proteins expressed in transgenic plants are subjected to the delivery and modification processes present within plant cells. Here, it is demonstrated that unique membrane sequences deliver a yellow fluorescent protein (YFP) to the seed protein storage vacuoles in transgenic tobacco (Nicotiana tabacum L.) plants, where the YFP is then separated from its membrane anchors. This precise targeting and separation is required for the successful delivery of useful proteins to seed protein storage vacuoles for their stable accumulation in transgenic crops.

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