Synthesis of Oat Globulin Precursors

Brinegar, A. Chris; Peterson, David M.

doi:10.1104/pp.70.6.1767

Cited by 41 publications

(24 citation statements)

References 11 publications

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“…protein synthesis studies (4,12,23,26). Our present results from the in vivo labeling study of total globulin in developing oat groats support the previous observations.…”

Section: Adeli and Altosaarsupporting

confidence: 81%

“…Brinegar and Peterson (4) have recently reported similar observations. They suggested that the 58 to 62 kD polypeptides are the precursors of a anda globulin species with mol wt 38 kD and 21kD.…”

Section: Adeli and Altosaarsupporting

confidence: 67%

“…This suggests that post- ' translational processing of 60 to 62 kD precursors occurs to yield the a and ,B subunits. In vivo labeling studies have also shown the appearance of 58 to 62 kD polypeptides after short-period labeling of oat caryopses (4). RER is thought to be the site of synthesis for legume reserve proteins (2).…”

mentioning

confidence: 99%

“…The a and 1 subunits are apparently linked through disulfide bonds to form a dimer molecule with average mol wt 58,000 (3, 12, 21). Oat seed polysomes, when translated in vitro, give rise to two globulin polypeptides (60-62 kD) which are immunoprecipitable with globulin antibodies (4,12,23,26 …”

mentioning

confidence: 99%

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Role of Endoplasmic Reticulum in Biosynthesis of Oat Globulin Precursors

Adeli¹,

Altosaar²

1983

Plant Physiol.

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Oat (Avena sativa L.) groats were labeled with radioactive leucine and salt-soluble proteins were extracted and analyzed. Polyacrylamide gel electrophoresis followed by fluorography indicated two radioactive polypeptides with molecular weight 58 to 62 kilodaltons which were similar in size to unreduced globulin a-,8 dimers. The role of endoplasmic reticulum in the synthesis of these globulin polypeptides was investigated by in vivo and in vitro protein synthesis studies. Labeled tissue was fractionated by centrifugation and rough endoplasmic reticulum was isolated. Two polypeptides which had molecular weights of 58 to 62 kilodaltons and were immunoprecipitable with antiglobulin immunoglobulin G were found to be transiently associated with the endoplasmic reticulum. Rough endoplasmic reticulum, as well as membrane-bound polysomes, directed the in vitro synthesis of two polypeptides with molecular weight 58 to 62 kilodaltons corresponding in size to unreduced a-# dimers and could be immunoprecipitated with antiglobulin immunoglobulin G. The translation products of free polysomes did not show this. In pulse-labeling, globulin polypeptides with molecular weight 58 to 62 kilodaltons, as well as the a + , subunits, were labeled in protein bodies.The data suggest that oat globulin polypeptides are synthesized as higher molecular weight precursors on ER-associated polysomes. These precursors are probably transported into protein bodies and cleaved into smaller a and ,B subunits.Oat seeds begin to synthesize a group of salt-soluble globulin polypeptides during development from 9 daf;2 thereafter, these globulins are predominant in the seeds among the four Osborne fractions (18,21). At maturity, the globulin fraction constitutes up to 75% of total oat protein in the groat (18,20). This is a unique characteristic of oat since other cereals such as wheat, barley, rye, and maize contain alcohol-soluble prolamins as the major storage protein fraction (14). Oat globulin is found in mature grain as a 12S multimeric molecule with an average mol wt of 348,000 (17). This molecule consists of 6 dimers, each dimer containing a 35 (a) and a 22 (13) kD subunit (17). The a and 1 subunits are apparently linked through disulfide bonds to form a dimer molecule with average mol wt 58,000 (3, 12, 21). Oat seed polysomes, when translated in vitro, give rise to two globulin polypeptides (60-62 kD) which are immunoprecipitable with globulin antibodies (4,12,23,26

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“…protein synthesis studies (4,12,23,26). Our present results from the in vivo labeling study of total globulin in developing oat groats support the previous observations.…”

Section: Adeli and Altosaarsupporting

confidence: 81%

Section: Adeli and Altosaarsupporting

confidence: 67%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Role of Endoplasmic Reticulum in Biosynthesis of Oat Globulin Precursors

Adeli¹,

Altosaar²

1983

Plant Physiol.

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“…2a). Legumin in legumes (Croy et al, 1980;Spencer & Higgins, 1980;Barton et al, 1982), and leguminlike storage proteins in oats (Avena) (Brinegar & Peterson, 1982) and rice (Oryza) (Yamagata et al, 1982) are also synthesized from precursors in which the a-and fl-subunits are peptide-bonded.…”

mentioning

confidence: 99%

Assembly of Agrostemma githago (corn-cockle) storage proteins and their precursor proteins into oligomers

Klerk¹,

Engelen²

1985

Biochemical Journal

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The major fraction of seed storage proteins of Agrostemma githago (corn-cockle), a non-leguminous dicot, occurs as material with S20,w values of approximately 11S and approximately 2S, and a minor fraction as oligomers with S20,w values of approximately 6.5S. The 11S proteins are of the legumin type and consist of disulphide-linked α- and β-subunits of Mr approximately 39 000 and approximately 23 000 respectively. The oligomeric assembly of the precursor polypeptides of the 11S proteins was examined. The approximately 65 000-Mr precursor polypeptides of two 11S proteins, which consist of 38 000-25 000-Mr subunits and 36 000-22 000-Mr subunits respectively, were assembled into oligomers of approximately 7S and subsequently cleaved. Thereafter the 11S oligomer was formed. The 88 000-Mr precursor of a third 11S protein, which consists of 41 000-23 000-Mr subunits, was assembled into an approximately 8S oligomer and then cleaved, yielding two disulphide-linked intermediates of Mr 59 000 and 24 000. Thereafter, the 11S oligomer was formed. Processing of the 59 000-Mr to the 41 000-Mr polypeptide occurred both in the 8S and in the 11S form.

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Subunit structure of Vicia faba legumin and implications for the improvement of protein quality

Horstmann¹,

Müntz²

1986

Nahrung

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Legumin, the main storage protein of Viria faba seeds. consists of the two different subunit types A and B.Each subunit is composed of two polypeptide chains, one acidic (2) and one basic (p) linked by disulphide bridges. In each subunit type specific a-P-pairs occur. in type A 3-as well as 8-polypeptides contain methioninc, whereas in both the constituent polypeptides of type B subunits methionine is lacking. Since the specific r-B-pairs reflect their origin from a common precursor and hence from a single gene for each subunit, it seems worthwhile to look for Vicia varieties containing an increased ratio of type A/B subunits and therefore a legumin with a higher content of the nutritionally limiting amino acid methionine. Results of such a screening are presented.

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Synthesis of Oat Globulin Precursors

Cited by 41 publications

References 11 publications

Role of Endoplasmic Reticulum in Biosynthesis of Oat Globulin Precursors

Role of Endoplasmic Reticulum in Biosynthesis of Oat Globulin Precursors

Assembly of Agrostemma githago (corn-cockle) storage proteins and their precursor proteins into oligomers

Subunit structure of Vicia faba legumin and implications for the improvement of protein quality

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