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. 1988 Feb;85(4):1082–1085. doi: 10.1073/pnas.85.4.1082

A hydroxyproline-rich protein in the soybean cell wall.

V Averyhart-Fullard 1, K Datta 1, A Marcus 1
PMCID: PMC279708  PMID: 3422480

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bhown A. S., Mole J. E., Hunter F., Bennett J. C. High-sensitivity sequence determination of proteins quantitatively recovered from sodium dodecyl sulfate gels using an improved electrodialysis procedure. Anal Biochem. 1980 Mar 15;103(1):184–190. doi: 10.1016/0003-2697(80)90254-7. [DOI] [PubMed] [Google Scholar]
  2. Brysk M. M., Chrispeels M. J. Isolation and partial characterization of a hydroxyproline-rich cell wall glycoprotein and its cytoplasmic precursor. Biochim Biophys Acta. 1972 Feb 29;257(2):421–432. doi: 10.1016/0005-2795(72)90295-4. [DOI] [PubMed] [Google Scholar]
  3. Cassab G. I., Nieto-Sotelo J., Cooper J. B., van Holst G. J., Varner J. E. A developmentally regulated hydroxyproline-rich glycoprotein from the cell walls of soybean seed coats. Plant Physiol. 1985 Mar;77(3):532–535. doi: 10.1104/pp.77.3.532. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chen J., Varner J. E. An extracellular matrix protein in plants: characterization of a genomic clone for carrot extensin. EMBO J. 1985 Sep;4(9):2145–2151. doi: 10.1002/j.1460-2075.1985.tb03908.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chen J., Varner J. E. Isolation and characterization of cDNA clones for carrot extensin and a proline-rich 33-kDa protein. Proc Natl Acad Sci U S A. 1985 Jul;82(13):4399–4403. doi: 10.1073/pnas.82.13.4399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cooper J. B., Varner J. E. Cross-linking of soluble extensin in isolated cell walls. Plant Physiol. 1984 Oct;76(2):414–417. doi: 10.1104/pp.76.2.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dubray G., Bezard G. A highly sensitive periodic acid-silver stain for 1,2-diol groups of glycoproteins and polysaccharides in polyacrylamide gels. Anal Biochem. 1982 Jan 15;119(2):325–329. doi: 10.1016/0003-2697(82)90593-0. [DOI] [PubMed] [Google Scholar]
  8. Hong J. C., Nagao R. T., Key J. L. Characterization and sequence analysis of a developmentally regulated putative cell wall protein gene isolated from soybean. J Biol Chem. 1987 Jun 15;262(17):8367–8376. [PubMed] [Google Scholar]
  9. Horn M. E., Sherrard J. H., Widholm J. M. Photoautotrophic growth of soybean cells in suspension culture: I. Establishment of photoautotrophic cultures. Plant Physiol. 1983 Jun;72(2):426–429. doi: 10.1104/pp.72.2.426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kirschenbaum D. M. A compilation of amino acid analyses of proteins. II. Anal Biochem. 1972 Sep;49(1):248–266. doi: 10.1016/0003-2697(72)90264-3. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Lamport D. T., Katona L., Roerig S. Galactosylserine in extensin. Biochem J. 1973 May;133(1):125–132. doi: 10.1042/bj1330125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lamport D. T. The isolation and partial characterization of hydroxyproline-rich glycopeptides obtained by enzymic degradation of primary cell walls. Biochemistry. 1969 Mar;8(3):1155–1163. doi: 10.1021/bi00831a049. [DOI] [PubMed] [Google Scholar]
  14. Leach B. S., Collawn J. F., Jr, Fish W. W. Behavior of glycopolypeptides with empirical molecular weight estimation methods. 1. In sodium dodecyl sulfate. Biochemistry. 1980 Dec 9;19(25):5734–5741. doi: 10.1021/bi00566a011. [DOI] [PubMed] [Google Scholar]
  15. Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Stafstrom J. P., Staehelin L. A. Cross-linking patterns in salt-extractable extensin from carrot cell walls. Plant Physiol. 1986 May;81(1):234–241. doi: 10.1104/pp.81.1.234. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Stuart D. A., Varner J. E. Purification and Characterization of a Salt-extractable Hydroxyproline-rich Glycoprotein from Aerated Carrot Discs. Plant Physiol. 1980 Nov;66(5):787–792. doi: 10.1104/pp.66.5.787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. van Holst G. J., Varner J. E. Reinforced Polyproline II Conformation in a Hydroxyproline-Rich Cell Wall Glycoprotein from Carrot Root. Plant Physiol. 1984 Feb;74(2):247–251. doi: 10.1104/pp.74.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]

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