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Tissue- and stage-specific expression of a soybean (Glycine max L.) seed-maturation, biotinylated protein

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Abstract

A cDNA clone GmPM4 which encodes mRNA species in mature or dry soybean seeds was characterized. DNA sequence analysis shows that the deduced polypeptides have a molecular mass of 68 kDa. GmPM4 proteins have a relatively high amino acid sequence homology with a major biotinylated protein isolated from pea seeds, SBP65, but both of these proteins differ markedly from that of presently known biotin enzymes. The accumulation of GmPM4 mRNA is detectable in the leaf primodium and the vascular tissues of the hypocotyl-radicle axis of mature seeds, and the GmPM4 proteins are present at high levels in dry and mature soybean seeds, but not in fresh immature seeds. It degrades rapidly at the early stage of seed germination. These proteins are boiling-soluble and biotinylated when they are present endogenously in soybean seeds; however, the same recombinant protein expressed in Escherichia coli is boiling-soluble, but it is not biotinylated.

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Authors and Affiliations

  1. Institute of Botany, Academia Sinica, Taipei, T, aiwan

    Yue-ie C. Hsing, Chih-hua Tsou, Tze-fu Hsu, Zuey-ying Chen, Kim-leong Hsieh & Teh-yuan Chow

  2. Department of Agronomy, National Taiwan University, Taipei, Taiwan

    Jaw-shu Hsieh

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  1. Yue-ie C. Hsing
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  2. Chih-hua Tsou
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  3. Tze-fu Hsu
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  7. Teh-yuan Chow
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Hsing, Yi.C., Tsou, Ch., Hsu, Tf. et al. Tissue- and stage-specific expression of a soybean (Glycine max L.) seed-maturation, biotinylated protein. Plant Mol Biol 38, 481–490 (1998). https://doi.org/10.1023/A:1006079926339

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