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A Hydroxyproline-Rich Protein in the Soybean Cell Wall
V. Averyhart-Fullard, K. Datta and A. Marcus
Proceedings of the National Academy of Sciences of the United States of America
Vol. 85, No. 4 (Feb. 15, 1988), pp. 1082-1085
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30941
Page Count: 4
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A cDNA clone that hybridizes to an mRNA (1A10) that accumulates to a substantial level in the axis of the germinating soybean seed was sequenced. The amino acid sequence of the clone indicates an almost perfect repeat of Pro-Pro-Val-Tyr-Lys resulting in a protein containing 40% proline and lacking serine and histidine. On the likelihood that such a protein might be a hydroxyproline-rich cell-wall glycoprotein (HRGP), cell walls of a soybean cell culture were extracted by procedures used to obtain soluble basic cell-wall glycoproteins, and the proteins were fractionated and purified. A 33-kDa protein (and possibly a 28-kDa protein) was obtained that has an amino acid distribution similar to that of the cDNA clone. The protein lacks histidine and serine and contains 20% hydroxyproline and 20% proline. The HRGP is thus distinct both in its amino acid content and in its pentameric repeat of Pro-Pro-Val-Tyr-Lys, with half of the prolines being hydroxylated.
Proceedings of the National Academy of Sciences of the United States of America © 1988 National Academy of Sciences