The unique biosynthetic route from Lupinus beta-conglutin gene to blad

Research output: Contribution to journalArticle

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Abstract

Background: During seed germination, beta-conglutin undergoes a major cycle of limited proteolysis in which many of its constituent subunits are processed into a 20 kDa polypeptide termed blad. Blad is the main component of a glycooligomer, accumulating exclusively in the cotyledons of Lupinus species, between days 4 and 12 after the onset of germination. Principal Findings: The sequence of the gene encoding b-conglutin precursor (1791 nucleotides) is reported. This gene, which shares 44 to 57% similarity and 20 to 37% identity with other vicilin-like protein genes, includes several features in common with these globulins, but also specific hallmarks. Most notable is the presence of an ubiquitin interacting motif (UIM), which possibly links the unique catabolic route of b-conglutin to the ubiquitin/proteasome proteolytic pathway. Significance: Blad forms through a unique route from and is a stable intermediary product of its precursor, b-conglutin, the major Lupinus seed storage protein. It is composed of 173 amino acid residues, is encoded by an intron-containing, internal fragment of the gene that codes for beta-conglutin precursor (nucleotides 394 to 913) and exhibits an isoelectric point of 9.6 and a molecular mass of 20,404.85 Da. Consistent with its role as a storage protein, blad contains an extremely high proportion of the nitrogen-rich amino acids.
Original languageUnknown
Pages (from-to)e8542
JournalPLoS ONE
Volume5
Issue number1
DOIs
Publication statusPublished - 1 Jan 2010

Cite this

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title = "The unique biosynthetic route from Lupinus beta-conglutin gene to blad",
abstract = "Background: During seed germination, beta-conglutin undergoes a major cycle of limited proteolysis in which many of its constituent subunits are processed into a 20 kDa polypeptide termed blad. Blad is the main component of a glycooligomer, accumulating exclusively in the cotyledons of Lupinus species, between days 4 and 12 after the onset of germination. Principal Findings: The sequence of the gene encoding b-conglutin precursor (1791 nucleotides) is reported. This gene, which shares 44 to 57{\%} similarity and 20 to 37{\%} identity with other vicilin-like protein genes, includes several features in common with these globulins, but also specific hallmarks. Most notable is the presence of an ubiquitin interacting motif (UIM), which possibly links the unique catabolic route of b-conglutin to the ubiquitin/proteasome proteolytic pathway. Significance: Blad forms through a unique route from and is a stable intermediary product of its precursor, b-conglutin, the major Lupinus seed storage protein. It is composed of 173 amino acid residues, is encoded by an intron-containing, internal fragment of the gene that codes for beta-conglutin precursor (nucleotides 394 to 913) and exhibits an isoelectric point of 9.6 and a molecular mass of 20,404.85 Da. Consistent with its role as a storage protein, blad contains an extremely high proportion of the nitrogen-rich amino acids.",
keywords = "GLOBULINS, UBIQUITIN-INTERACTING MOTIF, VIGNA-UNGUICULATA SEEDS, 3-DIMENSIONAL STRUCTURE, MEMBERS, GERMINATION, BINDING, BEAN CANAVALIA-ENSIFORMIS, SEED STORAGE PROTEINS, LEGUME SEEDS",
author = "Ricardo Boavida",
note = "Monteiro, Sara, Freitas, Regina Rajasekhar BT Teixeira, Artur R. Ferreira RB",
year = "2010",
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volume = "5",
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The unique biosynthetic route from Lupinus beta-conglutin gene to blad. / Boavida, Ricardo.

In: PLoS ONE, Vol. 5, No. 1, 01.01.2010, p. e8542.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The unique biosynthetic route from Lupinus beta-conglutin gene to blad

AU - Boavida, Ricardo

N1 - Monteiro, Sara, Freitas, Regina Rajasekhar BT Teixeira, Artur R. Ferreira RB

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Background: During seed germination, beta-conglutin undergoes a major cycle of limited proteolysis in which many of its constituent subunits are processed into a 20 kDa polypeptide termed blad. Blad is the main component of a glycooligomer, accumulating exclusively in the cotyledons of Lupinus species, between days 4 and 12 after the onset of germination. Principal Findings: The sequence of the gene encoding b-conglutin precursor (1791 nucleotides) is reported. This gene, which shares 44 to 57% similarity and 20 to 37% identity with other vicilin-like protein genes, includes several features in common with these globulins, but also specific hallmarks. Most notable is the presence of an ubiquitin interacting motif (UIM), which possibly links the unique catabolic route of b-conglutin to the ubiquitin/proteasome proteolytic pathway. Significance: Blad forms through a unique route from and is a stable intermediary product of its precursor, b-conglutin, the major Lupinus seed storage protein. It is composed of 173 amino acid residues, is encoded by an intron-containing, internal fragment of the gene that codes for beta-conglutin precursor (nucleotides 394 to 913) and exhibits an isoelectric point of 9.6 and a molecular mass of 20,404.85 Da. Consistent with its role as a storage protein, blad contains an extremely high proportion of the nitrogen-rich amino acids.

AB - Background: During seed germination, beta-conglutin undergoes a major cycle of limited proteolysis in which many of its constituent subunits are processed into a 20 kDa polypeptide termed blad. Blad is the main component of a glycooligomer, accumulating exclusively in the cotyledons of Lupinus species, between days 4 and 12 after the onset of germination. Principal Findings: The sequence of the gene encoding b-conglutin precursor (1791 nucleotides) is reported. This gene, which shares 44 to 57% similarity and 20 to 37% identity with other vicilin-like protein genes, includes several features in common with these globulins, but also specific hallmarks. Most notable is the presence of an ubiquitin interacting motif (UIM), which possibly links the unique catabolic route of b-conglutin to the ubiquitin/proteasome proteolytic pathway. Significance: Blad forms through a unique route from and is a stable intermediary product of its precursor, b-conglutin, the major Lupinus seed storage protein. It is composed of 173 amino acid residues, is encoded by an intron-containing, internal fragment of the gene that codes for beta-conglutin precursor (nucleotides 394 to 913) and exhibits an isoelectric point of 9.6 and a molecular mass of 20,404.85 Da. Consistent with its role as a storage protein, blad contains an extremely high proportion of the nitrogen-rich amino acids.

KW - GLOBULINS

KW - UBIQUITIN-INTERACTING MOTIF

KW - VIGNA-UNGUICULATA SEEDS

KW - 3-DIMENSIONAL STRUCTURE

KW - MEMBERS

KW - GERMINATION

KW - BINDING

KW - BEAN CANAVALIA-ENSIFORMIS

KW - SEED STORAGE PROTEINS

KW - LEGUME SEEDS

U2 - 10.1371/journal.pone.0008542

DO - 10.1371/journal.pone.0008542

M3 - Article

VL - 5

SP - e8542

JO - PlosOne

JF - PlosOne

SN - 1932-6203

IS - 1

ER -