scholarly journals Combined Proteomic and Metabolomic Profiling of the Arabidopsis thaliana vps29 Mutant Reveals Pleiotropic Functions of the Retromer in Seed Development

2019 ◽  
Vol 20 (2) ◽  
pp. 362 ◽  
Author(s):  
Thomas Durand ◽  
Gwendal Cueff ◽  
Béatrice Godin ◽  
Benoît Valot ◽  
Gilles Clément ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Trafficking ◽  
Storage Proteins ◽  
Protein Sorting ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Seed Vigor ◽  
Seed Biology ◽  
Cargo Proteins ◽  
Vacuolar Protein

The retromer is a multiprotein complex conserved from yeast to humans, which is involved in intracellular protein trafficking and protein recycling. Selection of cargo proteins transported by the retromer depends on the core retromer subunit composed of the three vacuolar protein sorting (VPS) proteins, namely VPS26, VPS29, and VPS35. To gain a better knowledge of the importance of the plant retromer in protein sorting, we carried out a comparative proteomic and metabolomic analysis of Arabidopsis thaliana seeds from the wild-type and the null-retromer mutant vps29. Here, we report that the retromer mutant displays major alterations in the maturation of seed storage proteins and synthesis of lipid reserves, which are accompanied by severely impaired seed vigor and longevity. We also show that the lack of retromer components is counterbalanced by an increase in proteins involved in intracellular trafficking, notably members of the Ras-related proteins in brain (RAB) family proteins. Our study suggests that loss of the retromer stimulates energy metabolism, affects many metabolic pathways, including that of cell wall biogenesis, and triggers an osmotic stress response, underlining the importance of retromer function in seed biology.

scholarly journals Mobilization of seed storage proteins is crucial to high vigor in common bean seeds

2022 ◽  
Vol 52 (2) ◽  
Author(s):  
Natalia Carolina Moraes Ehrhardt-Brocardo ◽  
Cileide Maria Medeiros Coelho
Keyword(s):  
Storage Proteins ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Seed Vigor ◽  
Intensity Difference ◽  
Biochemical Component ◽  
Germination Process ◽  
Radicle Protrusion ◽  
Relationship Of

ABSTRACT: Seed germination is a complex process controlled by many factors, in which physical and biochemical mechanisms are involved and the mobilization of reserves is crucial for this process to occur. Although, seed reserve mobilization is usually thought to be a post-germination process, seed reserve proteins mobilization occurs during germination. This study quantified seed proteins of bean genotypes during different hydration times, in order to understand the process of protein mobilization and whether there is relationship of this biochemical component with seed vigor. This study was conducted using seeds with different levels of vigor, genotypes with highest (13, 42, 55 and 81) and lowest (07, 23, 44, 50, IPR-88-Uirapurú and Iapar 81) physiological quality. High vigor genotypes showed greater efficiency in hydrolysis and mobilization of protein component, because they presented low globulins content in cotyledons at radicle protrusion in relation to low vigor genotypes (07, 23 and 50). The protein alpha-amylase inhibitor, observed in all genotypes, is involved with the longer time needed for radicle protrusion, according to the band intensity difference in genotypes 07, 44 and Iapar 81.

scholarly journals Vacuolar sorting receptor for seed storage proteins in Arabidopsis thaliana

2003 ◽  
Vol 100 (26) ◽  
pp. 16095-16100 ◽  
Author(s):  
T. Shimada ◽  
K. Fuji ◽  
K. Tamura ◽  
M. Kondo ◽  
M. Nishimura ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Vacuolar Sorting Receptor ◽  
Vacuolar Sorting ◽  
Sorting Receptor

Generation of VHH antibodies against the Arabidopsis thaliana seed storage proteins

2013 ◽  
Vol 84 (1-2) ◽  
pp. 83-93 ◽  
Author(s):  
Thomas De Meyer ◽  
Dominique Eeckhout ◽  
Riet De Rycke ◽  
Sylvie De Buck ◽  
Serge Muyldermans ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Vhh Antibodies

scholarly journals Subunit E isoform 1 of vacuolar H+-ATPase OsVHA enables post-Golgi trafficking of rice seed storage proteins

2021 ◽  
Author(s):  
Jianping Zhu ◽  
Yulong Ren ◽  
Yuanyan Zhang ◽  
Jie Yang ◽  
Erchao Duan ◽  
...  
Keyword(s):  
Protein Trafficking ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Rice Seed ◽  
Ph Homeostasis ◽  
Rice Endosperm ◽  
Subunit E ◽  
Luminal Ph ◽  
Trafficking Defects

AbstractDense vesicles (DVs) are Golgi-derived plant-specific carriers that mediate post-Golgi transport of seed storage proteins in angiosperms. How this process is regulated remains elusive. Here, we report a rice (Oryza sativa) mutant, named glutelin precursor accumulation8 (gpa8) that abnormally accumulates 57-kDa proglutelins in the mature endosperm. Cytological analyses of the gpa8 mutant revealed that proglutelin-containing DVs were mistargeted to the apoplast forming electron-dense aggregates and paramural bodies in developing endosperm cells. Differing from previously reported gpa mutants with post-Golgi trafficking defects, the gpa8 mutant showed bent Golgi bodies, defective trans-Golgi network (TGN), and enlarged DVs, suggesting a specific role of GPA8 in DV biogenesis. We demonstrated that GPA8 encodes a subunit E isoform 1 of vacuolar H+-ATPase (OsVHA-E1) that mainly localizes to TGN and the tonoplast. Further analysis revealed that the luminal pH of the TGN and vacuole is dramatically increased in the gpa8 mutant. Moreover, the colocalization of GPA1 and GPA3 with TGN marker protein in gpa8 protoplasts was obviously decreased. Our data indicated that OsVHA-E1 is involved in endomembrane luminal pH homeostasis, as well as maintenance of Golgi morphology and TGN required for DV biogenesis and subsequent protein trafficking in rice endosperm cells.

scholarly journals MAIGO2 Is Involved in Exit of Seed Storage Proteins from the Endoplasmic Reticulum in Arabidopsis thaliana

2006 ◽  
Vol 18 (12) ◽  
pp. 3535-3547 ◽  
Author(s):  
Lixin Li ◽  
Tomoo Shimada ◽  
Hideyuki Takahashi ◽  
Haruko Ueda ◽  
Yoichiro Fukao ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Endoplasmic Reticulum ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins

scholarly journals Progressive Aggregation of 16 kDa Gamma-Zein during Seed Maturation in Transgenic Arabidopsis thaliana

2021 ◽  
Vol 22 (23) ◽  
pp. 12671
Author(s):  
Elsa Arcalis ◽  
Davide Mainieri ◽  
Alessandro Vitale ◽  
Eva Stöger ◽  
Emanuela Pedrazzini
Keyword(s):  
Arabidopsis Thaliana ◽  
Storage Proteins ◽  
Transgenic Arabidopsis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Maize Endosperm ◽  
Mature Embryos ◽  
Er Chaperone ◽  
Reducing Conditions ◽  
Mature Seeds

Prolamins constitute a unique class of seed storage proteins, present only in grasses. In the lumen of the endoplasmic reticulum (ER), prolamins form large, insoluble heteropolymers termed protein bodies (PB). In transgenic Arabidopsis (Arabidopsis thaliana) leaves, the major maize (Zea mays) prolamin, 27 kDa γ-zein (27γz), assembles into insoluble disulfide-linked polymers, as in maize endosperm, forming homotypic PB. The 16 kDa γ-zein (16γz), evolved from 27γz, instead forms disulfide-bonded dispersed electron-dense threads that enlarge the ER lumen without assembling into PB. We have investigated whether the peculiar features of 16γz are also maintained during transgenic seed development. We show that 16γz progressively changes its electron microscopy appearance during transgenic Arabidopsis embryo maturation, from dispersed threads to PB-like, compact structures. In mature seeds, 16γz and 27γz PBs appear very similar. However, when mature embryos are treated with a reducing agent, 27γz is fully solubilized, as expected, whereas 16γz remains largely insoluble also in reducing conditions and drives insolubilization of the ER chaperone BiP. These results indicate that 16γz expressed in the absence of the other zein partners forms aggregates in a storage tissue, strongly supporting the view that 16γz behaves as the unassembled subunit of a large heteropolymer, the PB, and could have evolved successfully only following the emergence of the much more structurally self-sufficient 27γz.

The role of mRNA and protein sorting in seed storage protein synthesis, transport, and deposition

2005 ◽  
Vol 83 (6) ◽  
pp. 728-737 ◽  
Author(s):  
Andrew J Crofts ◽  
Haruhiko Washida ◽  
Thomas W Okita ◽  
Mio Satoh ◽  
Masahiro Ogawa ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Storage Protein ◽  
Storage Proteins ◽  
Seed Storage Protein ◽  
Protein Localization ◽  
Protein Sorting ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Rna Localization ◽  
Endomembrane System

Rice synthesizes and accumulates high levels of 2 distinct classes of seed storage proteins and sorts them to separate intracellular compartments, making it an ideal model system for studying the mechanisms of storage protein synthesis, transport, and deposition. In rice, RNA localization dictates the initial site of storage protein synthesis on specific subdomains of the cortical endoplasmic reticulum (ER), and there is a direct relation between the RNA localization site and the final destination of the encoded protein within the endomembrane system. Current data support the existence of 3 parallel RNA localization pathways leading from the nucleus to the actively synthesizing cortical ER. Additional pathways may exist for the synthesis of cytoplasmic and nuclear-encoded proteins targeted to organelles, the latter located in a stratified arrangement in developing endosperm cells. The study of rice mutants, which accumulate unprocessed glutelin precursors, indicates that these multiple pathways prevent nonproductive interactions between different classes of storage proteins that would otherwise disrupt protein sorting. Indeed, it appears that the prevention of disruptive interactions between different classes of storage proteins plays a key role in their biosynthesis in rice. In addition to highlighting the unique features of the plant endomembrane system and describing the relation between RNA and protein localization, this minireview will attempt to address a number of questions raised by recent studies on these processes.Key words: mRNA localization, protein localization, endomembrane system, seed storage proteins, rice.

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