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THE PLANT CELL, Vol 1, Issue 9 945-952, Copyright © 1989 by American Society of Plant Biologists
Characterization of Two Soybean Repetitive Proline-Rich Proteins and a Cognate cDNA from Germinated Axes
K. Datta, A. Schmidt and A. Marcus
Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
We have resolved and analyzed two proline-rich proteins isolated from the
walls of soybean cells in culture. The proteins are similar in amino acid
content, containing 20% proline, 20% hydroxyproline, 20% lysine, 16%
valine, 10% tyrosine, and 10% glutamate. The proteins undergo a
rearrangement or a limited cleavage in dilute NaOH, but are otherwise
remarkably stable to a high concentration of alkali. We have cloned and
sequenced a cDNA from soybean axes germinated for 31 hours (1A10-2) coding
for a protein that closely corresponds in its amino acid content to that of
the proline-rich proteins. The cDNA sequence predicts a decameric repeat of
Pro-Pro-Val-Tyr-Lys-Pro-Pro-Val-Glu-Lys. Consequently, this class of
proteins is referred to as repetitive proline-rich proteins, i.e., RPRP2
and RPRP3. We have also analyzed RNA gel blots with probes that
discriminate between the new cDNA clone and a related cDNA previously
reported [SbPRP1; Hong, Nagao, and Key (1987). J. Biol. Chem. 262,
8367-8376]. Messenger RNAs from young seedlings and from soybean suspension
cultures correspond primarily to the new RPRP clone (1A10-2), whereas the
predominant mRNA accumulating later in the roots corresponds to SbPRP1.
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