Degradation of storage proteins in germinating seeds

Shutov, Andrei D.; Vaintraub, I. A.

doi:10.1016/s0031-9422(00)82245-1

Cited by 240 publications

(190 citation statements)

References 105 publications

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“…Several studies have shown the involvement of AP in the maturation process of storage proteins in concert with vacuolar processing enzyme (Runeberg-Roos et al 1994;Voigt et al 1997). Obtained data led to the hypothesis that the AP from seeds of P. vulgaris are strongly active in the beginning of germination, to initiate the breakdown of storage proteins, before the massive de novo biosynthesis of the CP (Shutov and Vaintraub 1987;Voigt et al 1997;Mutlu and Gal 1999). Indeed, germination appears to rise the level of CP (Bielawski et al 1994;Nguyen et al 1995;Sutoh et al 1999).…”

Section: Effect Of Copper Stress On Protease Classesmentioning

confidence: 99%

“…Maximum activity (100 %)015.12± 2.03 μg azocasein/min/g FW. The following buffers (0.1 M) were used for indicated pH ranges: Na-citrate, 4 to 5.5; Tris-maleate, 6 to 8.5; glycine, 9 and 9.5 proteases (Nielsen and Liener 1984) as well as MP (Belozersky et al 1990;Elpidina et al 1991) represent the major hydrolytic activities in bean cotyledons and are major factors controlling the degradation of storage proteins in germinating seeds (Shutov and Vaintraub 1987). However, upon Cu treatment, SH-proteases activity dependent abundance decreased dramatically as compared to the control pattern; 21 vs 56 % at 9th day.…”

Section: Effect Of Copper Stress On Protease Classesmentioning

confidence: 99%

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Proteolytic activities in Phaseolus vulgaris cotyledons under copper stress

Karmous

Khadija

Chaoui

et al. 2012

Physiol Mol Biol Plants

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The changes in the protease activities of bean cotyledons were investigated in response to copper stress. Assays using synthetic substrates and specific protease inhibitors followed by activity measurements and electrophoresis analysis allowed to study the classes of enzymes involved in the storage protein mobilization during the germination of bean (Phaseolus vulgaris L) seeds, and then identify which ones were affected in the presence of 200 μM CuCl 2 in the imbibition medium. Copper treatment affected embryo growth and total protease activity. The results of SDS-gelatin-PAGE show that Cu excess led to a decrease in protease activity of 45 to 66 kDa. Moreover, cysteine-, aspartic-and metallo-protease activities were markedly lowered under copper stress, while serine-protease one was enhanced as well as its activity dependent abundance in comparison with control. However, the relative distribution of major cysteine protease in H 2 O-germinated seeds was significantly diminished after Cu exposure. Thus, copper excess can disturb the nitrogen freeing from reserve tissues at enzymatic level; differential responses of protease classes are discussed, notably, cysteine protease in the way of storage protein mobilization and serine protease in protective mechanism one.

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Section: Effect Of Copper Stress On Protease Classesmentioning

confidence: 99%

Section: Effect Of Copper Stress On Protease Classesmentioning

confidence: 99%

Proteolytic activities in Phaseolus vulgaris cotyledons under copper stress

Karmous

Khadija

Chaoui

et al. 2012

Physiol Mol Biol Plants

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“…Degradation of these proteins in germinating seeds appears to follow a common pattern in many plant species (20). Hydrolysis of the proteins is initiated by the action of cysteine proteinases that cleave internal peptide bonds without causing extensive modifications.…”

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confidence: 99%

“…Evidence in support of this model comes from angiosperm as well as gymnosperm species (20). Vetch ( Vicia sativa L.) was one of the first species in which the components of this model were identified, isolated, and characterized (19).…”

mentioning

confidence: 99%

Purification and Characterization of Zein-Degrading Proteases from Endosperm of Germinating Maize Seeds

Barros¹,

Larkins²

1990

Plant Physiol.

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We have purified a group of four proteases (molecular mass 26-33 kilodalton) from germinating seeds of maize (Zea mays L. var W64A) using ammonium sulfate and isoelectric precipitations, anion exchange chromatography, and electroelution from preparative nondenaturing polyacrylamide gels. Their appearance in the endosperm of germinating seeds coincides with the onset of zein degradation. We have shown that these proteases degrade zeins dissolved in alcoholic solution as well as aggregated in protein bodies from developing maize kernels. The apparent molecular weights and net negative charges of each of these proteases are very similar. Additionally, they are inhibited by thiol-blocking agents and activated by reducing compounds. These characteristics suggest that they are a group of cysteine proteases involved in the first steps of storage protein degradation.Storage proteins provide nitrogen, sulfur, and carbon skeletons for the developing embryo during seed germination. Degradation of these proteins in germinating seeds appears to follow a common pattern in many plant species (20). Hydrolysis of the proteins is initiated by the action of cysteine proteinases that cleave internal peptide bonds without causing extensive modifications. The first cysteine proteinase to act, designated proteinase A, is synthesized de novo. The limited hydrolysis by proteinase A generates sites for the action of proteinase B, another type of cysteine proteinase, which is inactive against the native substrate. The carboxyl-ends exposed by the concerted action of proteinases A and B are attacked by carboxypeptidases, and these are normally serine proteases. Finally, tri-and dipeptides are degraded into amino acids by the action of amino-and dipeptidases.Evidence in support of this model comes from angiosperm as well as gymnosperm species (20). Vetch ( Vicia sativa L.) was one of the first species in which the components of this model were identified, isolated, and characterized (19). In mung bean (Vigna radiata L.), the proteolytic enzymes in germinating seeds were also extensively characterized (4), and most of the components of this model are recognized. In cereals, the pathway of storage protein degradation is not as well defined as in dicotyledons. However, the participation of proteinase A followed by the action of carboxypeptidases has been observed in several cereal species (20). 297In maize (Zea mays L.), the storage proteins comprise a group of alcohol-soluble polypeptides called zeins (6). Zeins accumulate in the endosperm during seed development and make up about 50% of total endosperm proteins in mature seeds. They can be divided into subclasses based on solubility and apparent molecular weights: a-zeins, molecular masses 19 and 22 kD, are readily soluble in 70% ethanol; y-, molecular masses 16 and 27 kD, (-, molecular mass 14 kD, and 6-zeins, molecular mass 10 kD, require reducing agents to be solubilized in ethanol (13).Zein degradation begins around the second DAG3, and by 8 DAG most of the protein in the endosp...

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“…First, legumin is attacked by protease A, synthesized during seedling growth, and only then protease B and some others, already present in dry seeds, enter into the hydrolysis [8].…”

Section: Resultsmentioning

confidence: 99%

In vitro reconstitution of the proteolytic system responsible for hydrolysis of the 13S globulin in buckwheat seeds

1993

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The reconstruction of the proteolytic system responsible for the profound hydrolyses of the mam storage protem of buckwheat seeds, 13s globulin, has been carried out in vitro. It was found that subsequent action of a metalloproteinase from dry buckwheat seeds and cysteine proteinase and carboxypeptidase from growing seedlings led to a profound hydrolysis of the storage protein. The 13s globuhn that was not hydrolyzed with metalloproteinase was not degraded by the proteolyttc enzymes of growing seedhngs. A scheme is proposed, which describes the functioning of the proteolytic system hydrolyzing the storage protein m growing buckwheat seedlings in vivo.

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Degradation of storage proteins in germinating seeds

Cited by 240 publications

References 105 publications

Proteolytic activities in Phaseolus vulgaris cotyledons under copper stress

Proteolytic activities in Phaseolus vulgaris cotyledons under copper stress

Purification and Characterization of Zein-Degrading Proteases from Endosperm of Germinating Maize Seeds

In vitro reconstitution of the proteolytic system responsible for hydrolysis of the 13S globulin in buckwheat seeds

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