Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1981 Jun 1;195(3):661–667. doi: 10.1042/bj1950661

The location of arabinosyl:hydroxyproline transferase in the membrane system of potato tissue culture cells.

R J Owens, D H Northcote
PMCID: PMC1162938  PMID: 6797402

Abstract

Incubation of a particulate preparation from potato tissue culture cells with UDP-beta-L-[1-3H] arabinose yielded a glycoprotein fraction containing labelled material with the characteristics of hydroxyproline arabinosides. The sugar-protein linkage was resistant to hot alkaline hydrolysis, and the hydrolytic products showed similar electrophoretic and chromatographic behavior to authentic hydroxyproline-arabinosides prepared from potato tissue culture cell walls. Incorporation of arabinose into glycoprotein was stimulated by the addition of de-arabinosylated potato lectin. The product of the incubation co-migrated with native potato lectin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The subcellular distribution of the arabinosyl-transferase was investigated by fractionating potato tissue culture membranes on a discontinuous sucrose gradient in the presence or absence of Mg2+. Under both fractionation conditions the highest specific activity of the enzyme was found in the Golgi-enriched fraction. The results are discussed in relation to the synthesis of the hydroxy-proline-rich glycoprotein component of plant cell walls.

Full text

PDF
661

Selected References

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

  1. Allen A. K., Desai N. N., Neuberger A., Creeth J. M. Properties of potato lectin and the nature of its glycoprotein linkages. Biochem J. 1978 Jun 1;171(3):665–674. doi: 10.1042/bj1710665. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Allen A. K., Neuberger A. The purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein. Biochem J. 1973 Oct;135(2):307–314. doi: 10.1042/bj1350307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baydoun E. A., Northcote D. H. Isolation and characterization of membranes from the cells of maize root tips. J Cell Sci. 1980 Oct;45:147–167. doi: 10.1242/jcs.45.1.147. [DOI] [PubMed] [Google Scholar]
  4. Bowles D. J., Kauss H. Characterization, enzymatic and lectin properties of isolated membranes from Phaseolus aureus. Biochim Biophys Acta. 1976 Sep 7;443(3):360–374. doi: 10.1016/0005-2736(76)90456-9. [DOI] [PubMed] [Google Scholar]
  5. Bretthauer R. K., Wu S. Synthesis of the mannosyl-O-serine (threonine) linkage of glycoproteins from polyisoprenylphosphate mannose in yeast (Hansenula holstii). Arch Biochem Biophys. 1975 Mar;167(1):151–160. doi: 10.1016/0003-9861(75)90451-8. [DOI] [PubMed] [Google Scholar]
  6. Chen W. W., Lennarz W. J., Tarentino A. L., Maley F. A lipid-linked oligosaccharide intermediate in glycoprotein synthesis in oviduct. Structural studies on the oligosaccharide chain. J Biol Chem. 1975 Sep 10;250(17):7006–7013. [PubMed] [Google Scholar]
  7. Dashek W. V. Synthesis and Transport of Hydroxyproline-rich Components in Suspension Cultures of Sycamore-Maple Cells. Plant Physiol. 1970 Dec;46(6):831–838. doi: 10.1104/pp.46.6.831. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dougall D. K., Shimbayashi K. Factors Affecting Growth of Tobacco Callus Tissue and Its Incorporation of Tyrosine. Plant Physiol. 1960 May;35(3):396–404. doi: 10.1104/pp.35.3.396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ecklund P. R., Moore T. C. Correlations of Growth Rate and De-etiolation with Rate of Ent-Kaurene Biosynthesis in Pea (Pisum sativum L.). Plant Physiol. 1974 Jan;53(1):5–10. doi: 10.1104/pp.53.1.5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fincher G. B., Sawyer W. H., Stone B. A. Chemical and physical properties of an arabinogalactan-peptide from wheat endosperm. Biochem J. 1974 Jun;139(3):535–545. doi: 10.1042/bj1390535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gamborg O. L. Aromatic metabolism in plants. II. Enzymes of the shikimate pathway in suspension cultures of plant cells. Can J Biochem. 1966 Jun;44(6):791–799. doi: 10.1139/o66-097. [DOI] [PubMed] [Google Scholar]
  12. Gardiner M., Chrispeels M. J. Involvement of the Golgi Apparatus in the Synthesis and Secretion of Hydroxyproline-rich Cell Wall Glycoproteins. Plant Physiol. 1975 Mar;55(3):536–541. doi: 10.1104/pp.55.3.536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Heath M. F., Northcote D. H. Glycoprotein of the wall of sycamore tissue-culture cells. Biochem J. 1971 Dec;125(4):953–961. doi: 10.1042/bj1250953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. KIVIRIKKO K. E. HYDROXYPROLINE-CONTAINING FRACTIONS IN NORMAL AND CORTISONE-TREATED CHICK EMBRYOS. Acta Physiol Scand Suppl. 1963:SUPPL 219–22092. [PubMed] [Google Scholar]
  15. KOLLAR S. J., JARAI M. Biochemical chlorination in Streptomvces aureofaciens. Nature. 1960 Nov 19;188:665–665. doi: 10.1038/188665a0. [DOI] [PubMed] [Google Scholar]
  16. KOLOR M. G., ROBERTS H. R. A new reagent for the detection of hydroxyproline on paper chromatograms. Arch Biochem Biophys. 1957 Aug;70(2):620–622. doi: 10.1016/0003-9861(57)90151-0. [DOI] [PubMed] [Google Scholar]
  17. Karr A. L. Isolation of an enzyme system which will catalyze the glycosylation of extensin. Plant Physiol. 1972 Aug;50(2):275–282. doi: 10.1104/pp.50.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Keegstra K., Talmadge K. W., Bauer W. D., Albersheim P. The Structure of Plant Cell Walls: III. A Model of the Walls of Suspension-cultured Sycamore Cells Based on the Interconnections of the Macromolecular Components. Plant Physiol. 1973 Jan;51(1):188–197. doi: 10.1104/pp.51.1.188. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. 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]
  21. 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]
  22. Lord J. M., Kagawa T., Moore T. S., Beevers H. Endoplasmic reticulum as the site of lecithin formation in castor bean endosperm. J Cell Biol. 1973 Jun;57(3):659–667. doi: 10.1083/jcb.57.3.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. NEUFELD E. F., FEINGOLD D. S., HASSID W. Z. Phosphorylation of D-galactose and L-arabinose by extracts from Phaseolus aureus seedlings. J Biol Chem. 1960 Apr;235:906–909. [PubMed] [Google Scholar]
  24. NEUFELD E. F., GINSBURG V., PUTMAN E. W., FANSHIER D., HASSID W. Z. Formation and interconversion of sugar nucleotides by plant extracts. Arch Biochem Biophys. 1957 Jul;69:602–616. doi: 10.1016/0003-9861(57)90524-6. [DOI] [PubMed] [Google Scholar]
  25. Nagahashi J., Beevers L. Subcellular Localization of Glycosyl Transferases Involved in Glycoprotein Biosynthesis in the Cotyledons of Pisum sativum L. Plant Physiol. 1978 Mar;61(3):451–459. doi: 10.1104/pp.61.3.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Northcote D. H. The involvement of the Golgi apparatus in the biosynthesis and secretion of glycoproteins and polysaccharides. Biomembranes. 1979;10:51–76. doi: 10.1007/978-1-4615-6564-2_2. [DOI] [PubMed] [Google Scholar]
  27. O'Neill M. A., Selvendran R. R. Glycoproteins from the cell wall of Phaseolus coccineus. Biochem J. 1980 Apr 1;187(1):53–63. doi: 10.1042/bj1870053. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Pope D. G. Relationships between Hydroxyproline-containing Proteins Secreted into the Cell Wall and Medium by Suspension-cultured Acer pseudoplatanus Cells. Plant Physiol. 1977 May;59(5):894–900. doi: 10.1104/pp.59.5.894. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Ray P. M., Shininger T. L., Ray M. M. ISOLATION OF beta-GLUCAN SYNTHETASE PARTICLES FROM PLANT CELLS AND IDENTIFICATION WITH GOLGI MEMBRANES. Proc Natl Acad Sci U S A. 1969 Oct;64(2):605–612. doi: 10.1073/pnas.64.2.605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Sharma C. B., Babczinski P., Lehle L., Tanner W. The role of dolicholmonophosphate in glycoprotein biosynthesis in Saccharomyces cerevisiae. Eur J Biochem. 1974 Jul 1;46(1):35–41. doi: 10.1111/j.1432-1033.1974.tb03594.x. [DOI] [PubMed] [Google Scholar]
  31. Shore G., Maclachlan G. A. The site of cellulose synthesis. Hormone treatment alters the intracellular location of alkali-insoluble beta-1,4-glucan (cellulose) synthetase activities. J Cell Biol. 1975 Mar;64(3):557–571. doi: 10.1083/jcb.64.3.557. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES