Soybean proteins/peptides: A review on their importance, biosynthesis, vacuolar sorting, and accumulation in seeds.

Soybean is one of the most important sources of plant protein and is known for its wide range of agricultural, food, and industrial applications as well as health benefits. Interest in soybean proteins has been steadily growing as progressively more applications and benefits are discovered. This review article is focused on the major seed storage proteins of soybean, their three-dimensional structures, their nutritional importance and bioactive peptides, cellular synthesis, and accumulation in seeds.

Structure of the post-translational protein translocation machinery of the ER membrane.

Many proteins must translocate through the protein-conducting Sec61 channel in the eukaryotic endoplasmic reticulum membrane or the SecY channel in the prokaryotic plasma membrane. Proteins with highly hydrophobic signal sequences are first recognized by the signal recognition particle (SRP) and then moved co-translationally through the Sec61 or SecY channel by the associated translating ribosome. Substrates with less hydrophobic signal sequences bypass the SRP and are moved through the channel post-translationally.

A Molecular Target for an Alcohol Chain-Length Cutoff.

Despite the widespread consumption of ethanol, mechanisms underlying its anesthetic effects remain uncertain. n-Alcohols induce anesthesia up to a specific chain length and then lose potency-an observation known as the "chain-length cutoff effect." This cutoff effect is thought to be mediated by alcohol binding sites on proteins such as ion channels, but where these sites are for long-chain alcohols and how they mediate a cutoff remain poorly defined.

Gly m 5/Gly m 8 fusion component as a potential novel candidate molecule for diagnosing soya bean allergy in Japanese children.

Background: Soya bean is a major food allergen in children. Component-resolved diagnostics has improved the accuracy of diagnosing immunoglobulin E (IgE)-mediated food allergies.

Objective: We aimed to develop a novel component for the diagnosis of soya bean allergy using recombinant technology.

A Soluble Fluorescent Binding Assay Reveals PIP Antagonism of TREK-1 Channels.

Lipid regulation of ion channels by low-abundance signaling lipids phosphatidylinositol 4,5-bisphosphate (PIP) and phosphatidic acid (PA) has emerged as a central cellular mechanism for controlling ion channels and the excitability of nerves. A lack of robust assays suitable for facile detection of a lipid bound to a channel has hampered the probing of the lipid binding sites and measuring the pharmacology of putative lipid agonists for ion channels. Here, we show a fluorescent PIP competition assay for detergent-purified potassium channels, including TWIK-1-related K-channel (TREK-1).

Stable accumulation of seed storage proteins containing vaccine peptides in transgenic soybean seeds.

There has been a significant increase in the use of transgenic plants for the large-scale production of pharmaceuticals and industrial proteins. Here, we report the stable accumulation of seed storage proteins containing disease vaccine peptides in transgenic soybean seeds. To synthesize vaccine peptides in soybean seeds, we used seed storage proteins as a carrier and a soybean breeding line lacking major seed storage proteins as a host.

Development of a novel transgenic rice with hypocholesterolemic activity via high-level accumulation of the α' subunit of soybean β-conglycinin.

Soybean 7S globulin, known as β-conglycinin, has been shown to regulate human plasma cholesterol and triglyceride levels. Furthermore, the α' subunit of β-conglycinin has specifically been shown to possess low-density lipoprotein (LDL)-cholesterol-lowering activity. Therefore, accumulation of the α' subunit of β-conglycinin in rice seeds could lead to the production of new functional rice that could promote human health.

Differential expression and elution behavior of basic 7S globulin among cultivars under hot water treatment of soybean seeds.

Basic 7S globulin (Bg7S), which accumulates in mature soybean (Glycine max) seeds, is an extracellular matrix protein. A large amount of Bg7S is synthesized de novo and is eluted from soybean seeds when immersed in 50-60°C water (hot water treatment, HWT). However, the Bg7S elution mechanism remains unclear.

High-level production of lactostatin, a hypocholesterolemic peptide, in transgenic rice using soybean A1aB1b as carrier.

Hypercholesterolemia, a form of cardiovascular disease, is one of the leading causes of deaths worldwide. Lactostatin (Ile-Ile-Ala-Glu-Lys), derived from β-lactoglobulin in cow's milk, is a bioactive peptide with hypocholesterolemic activity higher than sitosterol, a known anti-hypercholesterolemic drug. Here, we successfully developed a transgenic rice accumulating a much higher level of lactostatin by inserting 29 IIAEK sequences into the structurally flexible (nonconserved) regions of soybean seed storage protein, A1aB1b, and introducing it into LGC-1 (low glutelin content mutant 1) as host variety.

Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: insight into its physico-chemical properties.

Amaranth is a crop known for its high quality proteins. 11S Globulin is one of the most abundant and important storage proteins of the amaranth grain. Here, we report the crystal structure of amaranth 11S proglobulin at a final resolution of 2.

Crystal structure of the major peanut allergen Ara h 1.

Ara h 1, a 7S globulin, is one of the three major peanut allergens. We previously reported the crystallization of the core region of recombinant Ara h 1. Here, we present the crystal structure of the Ara h 1 core at a resolution of 2.

Expression and purification of peanut oleosins in insect cells.

Oleosins contain a unique hydrophobic domain which is inserted into the oil matrix and are involved in the formation and stability of plant oil bodies. These proteins have also been reported to possess some allergenic properties. Therefore, knowledge of its three-dimensional structure is vital for further structural and immunological characterization.

Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region.

Peanuts contain some of the most potent food allergens known to date. Ara h 1 is one of the three major peanut allergens. As a first step towards three-dimensional structure elucidation, recombinant Ara h 1 core region was cloned, expressed in Escherichia coli and purified to homogeneity.

Development of transgenic rice containing a mutated beta subunit of soybean beta-conglycinin for enhanced phagocytosis-stimulating activity.

Improving the nutraceutical value of rice would positively impact the health and well-being of rice consumers worldwide. Based on the three-dimensional structure of soybean beta-conglycinin, we designed a beta subunit with a strong phagocytosis-stimulating activity (mbeta subunit). Here, we describe the genetic modification and production of rice seeds containing the mbeta subunit as part of our aim to develop a food material that promotes human health.

Expression, purification, cross-reactivity and homology modeling of peanut profilin.

Plant profilins are known pan-allergens involved in the cross-reactions between pollen and plant foods. Peanut profilin, Ara h 5, is one of the important peanut allergens. Presently, most immunological, biochemical and structural studies on peanut allergens have focused on the three major allergens (Ara h 1, 2 and 3).

Conservation and divergence on plant seed 11S globulins based on crystal structures.

The crystal structures of two pro-11S globulins namely: rapeseed procruciferin and pea prolegumin are presented here. We have extensively compared them with the other known structures of plant seed 11S and 7S globulins. In general, the disordered regions in the crystal structures among the 11S globulins correspond to their five variable regions.

Carbohydrate moieties contribute significantly to the physicochemical properties of french bean 7s globulin phaseolin.

We have previously reported that the solubility of French bean 7S globulin (phaseolin) at low ionic strength and its emulsifying stability are remarkably high compared with those of 7S globulins prepared from other plant species, including soybean (Kimura et al. J. Agric.