Molecular and Subunit Heterogeneity of Legumin of<i>Pisum sativum</i>L. (Garden Pea)— A Multi-Dimensional Gel Electrophoretic Study

Matta, N. K.; Gatehouse, John A.; Boulter, D.

doi:10.1093/jxb/32.6.1295

Cited by 78 publications

(24 citation statements)

References 12 publications

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“…It is also possible that the'two forms ofcDNA represent transcripts from two different types of gene, especially as there are known to be several copies of the legumin gene in the pea genome (8). Such a hypothesis is in agreement with the observation that there are several size classes of legumin acidic subunits in peas although the sizes of the basic subunits are fairly constant (3,19). Insertions or deletions in the genes may account for this heterogeneity in the proteins.…”

Section: G G L R I I S P P E K K Q a R H Q R G S R Q E E D E D E E K supporting

confidence: 54%

“…The purified protein was separated into a and fl subunits by ion exchange chromatography in the presence of 8 M urea and 1 mM dithiothreitol on DEAE-cellulose as described (4). The major t~-subunit peak containing only the o~-subunits of the subunit pairs previously designated L4 (19) or t~ M (3) was collected. Separation of the different/3-subunits was not carried out.…”

Section: Methodsmentioning

confidence: 99%

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Two cDNA clones coding for the legumin protein of Pisum sativum L. contain sequence repeats

et al. 1984

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The sequence of two cDNA clones coding for the whole of the β-subunit and most of the α-subunit of legumin are presented together with a considerable amount of protein sequence data to confirm the predicted amino acid sequence. A unique feature shown by these cDNAs is the presence of three 56 base pair tandem repeats in the region encoding the C terminal of the α polypeptide. The tandem repeats are also exhibited in the predicted polypeptide sequence as three 18 amino acid repeats which contain extremely high proportions of polar, mainly acidic, residues. The new sequences are compared to the previously published sequence of some shorter legumin cDNAs (Nature 295: 76-79). In the region where the sequences overlap, the previous cDNAs differ from the new ones by only a few base substitutions but most of the repeated region is not present though the sequences on either side are. The possibility that the absence of the repeats may reflect the difference between two types of legumin gene, rather than an artefact of the cloning of the cDNAs, is discussed.

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Section: G G L R I I S P P E K K Q a R H Q R G S R Q E E D E D E E K supporting

confidence: 54%

Section: Methodsmentioning

confidence: 99%

Two cDNA clones coding for the legumin protein of Pisum sativum L. contain sequence repeats

et al. 1984

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“…In pea seeds the mature legumin protein consists of an ct polypeptide (M r = 38 000) disulphide-bonded to a ~ polypeptide (M r = 21000) [7,30,33]. The legumin deposited in seeds of a transformed N.…”

Section: Polypeptide Composition Of Leguminmentioning

confidence: 99%

“…The arrows indicate the unreduced 58 kDa (A) and reduced 38 kDa and 21 kDa (B) polypeptide products of the LegA gene [6]. The other bands seen in both A and B tracks represent products of the other 8 expressed members of the pea legumin gene family -see details in [6] and [33].…”

Section: Polypeptide Composition Of Leguminmentioning

confidence: 99%

Tissue-specific expression of a pea legumin gene in seeds of Nicotiana plumbaginifolia

et al. 1988

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A 3.4-kilobase genomic DNA fragment from Pisum sativum L. containing the LegA gene, which encodes a major legumin storage protein, was transferred to Nicotiana plumbaginifolia using an Agrobacterium tumefaciens strain containing the Bin 19 binary vector system. Northern hybridisation analysis of legA-transformed plants demonstrated that legumin-specific RNA was present in developing seeds but not in developing leaves. Legumin protein was immunologically detected in the mature seeds of legA-transformed plants, and was present as the correct-size protein composed of disulphide-bonded polypeptides. It is concluded that the transferred pea genomic fragment contains all the information necessary for seed-specific expression of the legA gene, and for correct processing of the primary transcript and the precursor legumin protein.

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“…It is known to be a characteristic to legumin group proteins that basic subunits are highly conserved in size and sequence and that the acidic subunits are much more heterogeneous. 7 The reactivity of intramolecular disulfide bonds in red kidney bean protein was estimated by the mBBr labeling test (Fig. 2B).…”

mentioning

confidence: 99%

A Pepsin-Resistant 20 kDa Protein Found in Red Kidney Bean (Phaseolus vulgarisL.) Identified as Basic Subunit of Legumin

Momma¹

2006

Bioscience, Biotechnology, and Biochemistry

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Molecular and Subunit Heterogeneity of Legumin ofPisum sativumL. (Garden Pea)— A Multi-Dimensional Gel Electrophoretic Study

Cited by 78 publications

References 12 publications

Two cDNA clones coding for the legumin protein of Pisum sativum L. contain sequence repeats

Two cDNA clones coding for the legumin protein of Pisum sativum L. contain sequence repeats

Tissue-specific expression of a pea legumin gene in seeds of Nicotiana plumbaginifolia

A Pepsin-Resistant 20 kDa Protein Found in Red Kidney Bean (Phaseolus vulgarisL.) Identified as Basic Subunit of Legumin

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