دسته مقاله : مقالات لاتین
گروه : زراعت غلات - بیوشیمی گیاهی - فیزیولوژی گیاهان
whereas the products of co2 assimilation are deposited in plants in the
from of oligo-and polysaccharides as discussed in chapter 9the amino acids formed as products of nitrate assimilation are stored as proteins this are mostly special storage proteine which have no . enzymatic activity and are often deposited in the cell within protein bodies
protein bodies are enclosed by a single membrane and are derived from the endomembrane system of the endoplasmic reticulum and the golgi apparatus or the vacuoles. in potato tubers storage proteins are also stored in the vacuole
stems and roots they are stored in seeds and tubersand also in the cambium of tree trunks during winter to enable the rapid formation of leaves during seed germination and sprouting.
storage proteins are located in the endosperm in cereal seeds and in the cotyledons of most of the legume seeds.
whereas in cereals the protein content amounts to 10% to 15% of the dry weight in some legumes it is as high as 40 to 50 about 85 of these proteins are storage proteins
globally about 70% of the human demand for protein is met by the consumption of seeds either directly or indirectly by feeding them to animal for meat production therefore plant storage proteins are the basis for human nutrition however in many plant storage proteins the content of certain amino acids essential for the nutrition of humans and animals is too low in cereals for example the storage proteins are deficient in threonine tryptophan and particularly lysine whereas in legumes there is adeficiency of mehionine. since these amino acids cannot be synthesized by human metabolism humans depend on being supplied with them in their food
in humans with an entirely vegetarian diet such amino acid deficiencies can lead to irreparable physical and mental damage especially in childeren. it can also be aserious problem in pig and poultry feed. a target of research in plant genetic engineering is to improve the amino acid composition of the storage proteins of harvest products
scientists have long been interested in plant proteines by 1745 the italian ()already had isolated proteins from wheat. in 1924, at the connecticut agricultural experimental station, t. b. osborne classified plant proteins according to their solubility properties.he fractionated plant proteins into albumins (soluble in pure water ), globulins (soluble in diluted salt solutions), glutelins (soluble in diluted solutions of alkali and acids), and prolamins (soluble in aqueous ethanol).
when the structures of these proteins were determined later, it turned out that glutelins and prolamins were structurally closely related. therefore, in more recent literrature, glutelins are regarded as members of the group of prolamins. table 14.1shows some examples of various plant storage proteins.
14.1 globulins are the most abundant storage proteins
storage globulins occur in varying amounts in practically all plants. the most important globulins belong to the legumin and groups. both of these globulins are encoded by amultigene family.these multigene families descend from a common ancestor. legumin is the main storage protein of leguminous seeds. in broad bean, for instance, 75% of the total storage protein consists of legumin. legumin is a hexamer with a molecular mass of 300to 400 k da. the monomers contain two diffrent peptide chains ( ) which are linked by a disulfide bridge. the large alfa-chain usually has a molecular mass of about 35 to 40 k da, and the small beta-chain has a molecular mass of about 20 k da. hexamers can be composed of different ( )monomers. some contain methionine, whereas other do not. in the hexamer, the protein molecules are arranged in avery regular package and can be deposited in this form in the protein bodies. protein molecules, in which some of the protein chains are not properly folded, do not fit into this package and are degraded by peptidases. although it is relatively easy nowadays to exchang amino acids in a protein by genetic engineering, this has turned out to be difficult in storage proteins. as both the folding and the three-dimensional structure of the molecule may be altered by such exchange. recent progress in obtaining crystals enabled the analysis of the three-dimensional protein structure of the precursor trimers as well as of the mature storage proteins. these studies revealed that the stability of the storage proteins toward the proteases in the storage vacuoles is due to the fact that possible cleavage sites are hidden within the protein structure and in this way are protected against proteolysis.
vicilin shows similarities in its amino acid sequence to legumine, but occurs mostly as a trimer, of which the monomers consist of only one peptidechain. due to the lack of cystenine, the vicillin monomers are unable to form s-s bridges. in contrast legumins, viclins are often glycosylated: they contain carbohydrate residues,such as mannose, glucose, and n-acetylglucosamine.
14.2 prolamins are formed as storage proteins in grasses.
prolamins are contained only in grasses, such as cereals. they are present as a polymorphic mixture many different subunits of 30to 90 kda each. some of these subunits contain cysteine residues and are linked by s-sbridges. also in glutenin, which occurs in the grains of wheat and rye, monomers are linked by s-sbridges. the glutenin molecules differ in size. the suitability of flour for bread-making depends on the content of high molecular glutenins, and therefore flour from barley, oat, ormaize lacking glutenin, is not suitable for baking bread. since the glutenin content is a critical factor in determining the quality of bread grain, investigations are progress to improve the glutenin content of bread grain by genetic engineering.
14.3 2s-proteins are present in seeds of dicot plants.
2s-proteins are also widely distributed storage proteins. they represent a heterogeneous group of proteins, of which the sole definition is their sedimentation coefficient of about 2 svedberg(s). investigations of their structure have revealed that most 25-proteins have an interrelated structure and are possibly derived, along with the prolamins, from a common ancestor protein. napin, the predominant storage protein in rapeseed, is an example of a 25-protein is of substantial economic importanc since, after the oil has been extracted, the remainder of the rapeseed is used as fodder, napin and other related 25-proteins consist of two relatively small polypeptide chains of 9 k da and12 k da,which are linked by s-s bridges. so far, little is know about the packing of the prolamins and 25-proteins in the protein bodies.
14.4 special proteins protect seeds from being eaten by animals.
the protein bodies of some seeds contain other proteins, which, although also acting as storage proteins, protect the seeds from being eaten. to give some examples: the storage protein vieillin has a defense function by binding to the chitin matrix of fungi and insects. in some insects, it interferes with the development of the larvae. the seeds of some legumes contain leetins, which bind to sugar residues, irrespective of whether these are free sugarsor constituents of glycolipids or glycoproteins. when these seeds are consumed by animals, the lectins bind to glycoproteins in the intestine and thus interfere with the absorption of food. the seeds of some legumes and other plans also contain proteinase inhibitors, which block the digestion of proteins by inhibiting proteinases in the animal digestive tract. because of their content of lectins and proteinase inhibitors, many beans and other plant products are suitable for human consumption only after denaturing by cooking. this is one reason why humans have learned to cook. castor beans contain the extremely toxic protein ricin. a few mg of it can kill a human. beans also contain amylase inhibitors, which specifically inhibit the hydrolysis of starch by amylases in the digestive tract of certain insects.
using genetic engineering, alpha-amylase inhibitors from beans successfully expressed in the seeds of pea. whereas the larvae of the pea beetle normally cause large losses during storage of peas, the peas from the genetically engineered plants were protected against losses.
14.5 synthesis of the storage proyeins occurs at the rough endoplasmic reticulum
seed storage proteins are formed by ribosomes at the rough endoplasmic reticulum (er) (fig.14.1). the newly synthesized proteins occur in the lumen of the er, and the storage proteins are finally deposited in the protein bodies. in the case of 2s-proteins and prolamins, the protein bodies are formed by budding from the er membrane. the globulins are mostly transferred from the er by vesicle transfer via the golgi apparatus (section 1.6). first to the vacuole, from which protein bodies are formed by fragmentation. there also exists a pathway by which certain proteins (e.g.,globulins in wheat endosperm ) are transported directly by vesicle transfer from the er membrane to the vacuole without passing the golgi apparatus.
figure 14.2 shows the formatiom of legumin in detail. the protein formed by the ribosome contains at the n - terminus of the polypeptide chain a hydrophobic section called a signal sequence. after the synthesis of this signal sequence, translation comes to a halt, and the signal sequence forms a complex with three other components:
1- a signal recognition particle,
2-a binding protein located on the er membrane, and
3- a pore protein present in the er membrane.
the formation of this complex results in opening a pore in the er membrane: translation comtinues and the newly formed protein chain (e.g. pre pro legumin ) reaches the lumen of the er and anchors the ribosome on the er membrane for the duration of protein synthesis. immediately after the peptide chain enters the lumen, the signal sequence is removed by a signal peptidase located on the inside of the er membrane. the remaining polypeptide, termed a pro - legumin,contains the future alpha - and beta - chains of the legumin. an s-s linkage within the pro - legumin is formed in the er lumen. three pro - legumin molecules form a trimer, facilitated by chaperones.during this association, a quality control occurs: trimers without the correct conformation are degraded. the trimers are transferred via the golgi apparatus to the vacuoles, where the alpha- and bete - chains are separated by a peptidase. the subunits of the legumins assemble to hexamers and are deposited in this form. the protein bodies the final storage site of the legumins are derived from fragmentation of the vacuole. the carbohydrate chains of glycosylated vicilins (e.g of the phaesonlins from the bean phaseolus vulgaris ) are processed in the golgi apparatus.
the pre-pro-forms of newly synthesized 2s- proteins and prolamins which occur in the lumen of the er also contain a signal sequence. completion and aggregation of these proteins takes place in the lumen of the er from which the protein bodies are formed by budding.
14.6 proteinases mobilize the amino acids deposited in storage proteins
our knowledge about the mobilization of the amino acids from the storage proteins derives primarily from investigations of processes during seed germination. in most cases germination is induced by the uptake of water causing the protein bodies to form a vacuole. the hydrolysis of the storage proteins is catalyzed by proteinases which are in part deposited as inactive pro - forms together with the storage proteins in the protein bodies. other proteinases are synthesized anew and transferred via the lumen of the er and the golgi apparatus to the vacuoles (fig.14.2). these enzymes are synthesized initially as inactive pro - forms. activation of these pro - proteinases proceeds by limited proteolysis, in which a section of the sequence is removed by a specific peptidase. the remainder of the polypeptide represents the active proteinase.
the degradation of the storage proteins is also initiated by limited proteolysis. a specific proyeinase first removes small section of the protein sequence resulting in a change in the conformation of the storage protein. in cereal grains s-s bridges of storage proteins are cleaved by reduced thioredoxin (section 6.6) the unfolded is then susceptible to hydrolysis by various proteinases : for example, exopeptidases, which split off amino acids one after the other from the end protein molecule and endopeptidases which cleave within the molecule. in this way storage proteins are completely degraded in the vacuole and the liberated amino acids are provided as building material to the germinating plant.
glycerolipids are membrane constituents and function as carbon stores
glycerolipids are fatty acid esters of glycerol (fig. 15.1). triacylglycerols ( also called triglycerides ) consist of a glycerol molecule that is esterified with three fattyacids. in contrast to animals in plants triacylglycerols do not serve as an energy store but mainly as a carbon store in seeds and they are used as vegetable oils. in polar glycerolipids the glycerol is esterified with only two fatty acid and ahydrophilic group is linked to the thired -- oh group. these polar lipids are the main constituent of membranes.
14.1 there are three ways of deppsiting storageproteins in proteinbodies. A. in the formation of prolamins in cereal grains the prolamin aggregates in the lumen of the ER and the protein bodies are formed by budding off from the ER membrane. B. the proteins appearing in the lumen of the ER are transferred via the Golgi apparatus to the vacuole. the protein bodies are formed by fragmentation of the vacole. this is probably the most common pathway. C.the protein appearing in the lumen of the er are directly transferred to the vacuole circumventing the golgi apparatus.
figur14.2 legumin synthesis. the pre - form of the legumin ( pre pro legumin )formed by the ribosome is processed first in the lumen of the er and then further in the vacuole to give the end product.
figur 15.1 triacylglycerols containing three fatty acids are of a nonpolar nature. in contrast polar lipids are amphiphilic substances since besides the hydrophobic tail consisting of two fatty acids they contain a hydrophilic head.
درحالی که محصولات co2جذب شده درگیاهان به صورت پلی ساکاریدoligoتشکیل شده است بطوریکه درفصل 9بحث نمودیم اسیدآمینه هامحصولات جذبی نیترات راکه ذخیره شده اند بطوریکه این نوع پروتین ذخیره ای مخصوص پروتین هاست اغلب فعالیت enzymaticدرسلول مدت ها پروتین ساختاری توسط یک غشاجداقرارداده شده اندوendomembrance