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Uncleaved legumin in developing maize endosperm: identification, accumulation and putative subcellular localization.

Tomomi Yamagata1, Hisanao Kato, Satoshi Kuroda

  • 1Laboratory of Molecular Cell Biology, Department of Biological Resources, Faculty of Agriculture, Ehime University, Matsuyama 790-8566, Japan.

Journal of Experimental Botany
|February 25, 2003
PubMed
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Researchers identified a 51 kDa legumin-1 protein in maize endosperm protein bodies. Unlike in other plants, this maize protein is not cleaved into subunits, likely due to a missing cleavage sequence, and is most abundant in wild-type maize.

Area of Science:

  • Plant Molecular Biology
  • Maize Genetics
  • Protein Biochemistry

Background:

  • Maize (Zea mays L.) endosperm contains various protein bodies crucial for nutritional value.
  • Identifying novel proteins and their processing pathways is essential for understanding seed development and composition.

Purpose of the Study:

  • To identify and characterize a 51 kDa protein found in small protein bodies of maize endosperm.
  • To investigate the post-translational processing and abundance of this protein in different maize varieties.

Main Methods:

  • Protein extraction and fractionation from maize endosperm.
  • Peptide sequencing (V8 protease) and molecular cloning (3' and 5' PCR) to obtain full-length cDNA.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein analysis.

Related Experiment Videos

  • Transcript and protein level comparisons across maize varieties (wild-type, opaque-2, sweet corn).
  • Transmission electron microscopy (TEM) for protein body morphology.

    • Main Results:

    • A 51 kDa protein, identified as legumin-1, was isolated from small maize endosperm protein bodies.
    • Unlike in other species, legumin-1 in maize endosperm is not cleaved into 20 and 35 kDa subunits, despite a conserved cleavage site.
    • The lack of cleavage is attributed to the near absence of the canonical downstream cleavage sequence.
    • Legumin-1 transcript and protein levels are significantly higher in wild-type maize compared to opaque-2 and sweet corn varieties.
    • TEM revealed that legumin-1 resides in distinct protein bodies resembling those found in legumes.

    Conclusions:

    • Maize endosperm legumin-1 undergoes unique post-translational processing, remaining uncleaved due to sequence variations.
    • Differential expression of legumin-1 in maize varieties suggests genetic regulation impacting protein accumulation.
    • The morphology of legumin-1-containing protein bodies provides insights into seed protein storage mechanisms in maize.