Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 71, 2007 - Issue 9
Journal homepage
81
Views
8
CrossRef citations to date
0
Altmetric
Original Articles

In Vitro Stabilization and Minimum Active Component of Polygalacturonic Acid Synthase Involved in Pectin Biosynthesis

Takao OHASHIDepartment of Chemistry, Graduate School of Science, Osaka University
,
Takeshi ISHIMIZUDepartment of Chemistry, Graduate School of Science, Osaka University
,
Kazumasa AKITADepartment of Chemistry, Graduate School of Science, Osaka University
&
Sumihiro HASEDepartment of Chemistry, Graduate School of Science, Osaka University
Pages 2291-2299 | Received 18 May 2007, Accepted 30 May 2007, Published online: 22 May 2014

  • 1) Schols, H. A., and Voragen, A. G. J., The chemical structure of pectins. In “Pectins and Their Manipulation,” eds. Seymour, G. B., and Knox, J. P., Blackwell publishing, Oxford, pp. 1–29 (2002).
  • 2) O’Neill, M. A., and York, W. S., The composition and structure of plant primary cell walls. In “The Plant Cell Wall,” ed. Rose, J. K. C., Blackwell Publishing, Oxford, pp. 1–54 (2003).
  • 3) Schneider, G. G., and Bock, H., Über die Konstitution der Pektinstoffe. II. Mitteil.: Konstitution und Geleebildung. Ber. Deut. Chem. Ges., 71, 1353–1362 (1938).
  • 4) Ishii, T., O-Acetylated oligosaccharides from pectins of potato tuber cell walls. Plant Physiol., 113, 1265–1272 (1997).
  • 5) Needs, P. W., Rigby, N. M., Colquhoun, I. J., and Ring, S. G., Conflicting evidence for non-methyl galacturonosylesters in Daucus carota. Phytochemistry, 48, 71–77 (1998).
  • 6) Perrone, P., Hewage, C. M., Thomson, A. R., Bailey, K., Sadler, I. H., and Fry, S. C., Patterns of methyl and O-acetyl esterification in spinach pectins: new complexity. Phytochemistry, 60, 67–77 (2002).
  • 7) Mohnen, D., Biosynthesis of pectins. In “Pectins and Their Manipulation,” eds. Seymour, G. B., and Knox, J. P., Blackwell Publishing, Oxford, pp. 52–98 (2002).
  • 8) Ishimizu, T., and Hase, S., Pectin biosynthesis. In “Advances in Plant Physiology” Vol. 7, ed. Hemantaranjan, A., Scientific Publishers, Jodhpur, pp. 175–193 (2004).
  • 9) Bouton, S., Leboeuf, E., Mouille, G., Leydecker, M.-T., Talbotec, J., Granier, F., Lahaye, M., Höfte, H., and Truong, H.-N., QUASIMODO1 encodes a putative membrane-bound glycosyltransferase required for normal pectin synthesis and cell adhesion in Arabidopsis. Plant Cell, 14, 2577–2590 (2002).
  • 10) Orfila, C., Sorensen, S. O., Harholt, J., Geshi, N., Crombie, H., Truong, H. N., Reid, J. S. G., Knox, J. P., and Scheller, H. V., QUASIMODO1 is expressed in vascular tissue of Arabidopsis thaliana inflorescence stems, and affects homogalacturonan and xylan biosynthesis. Planta, 222, 613–622 (2005).
  • 11) Leboeuf, E., Guillon, F., Thoiron, S., and Lahaye, M., Biochemical and immunohistochemical analysis of pectic polysaccharides in the cell walls of Arabidopsis mutant QUASIMODO1 suspension-cultured cells: implications for cell adhesion. J. Exp. Bot., 56, 3171–3182 (2005).
  • 12) Sterling, J. D., Atmodjo, M. A., Inwood, S. E., Kolli, V. S. K., Quigley, H. F., Hahn, M. G., and Mohnen, D., Functional identification of an Arabidopsis pectin biosynthetic homogalacturonan galacturonosyltransferase. Proc. Natl. Acad. Sci. USA, 103, 5236–5241 (2006).
  • 13) Villemez, C. L., Lin, T.-Y., and Hassid, W. Z., Biosynthesis of the polygalacturonic acid chain of pectin by a particulate enzyme preparation from Phaseolus aureus seedlings. Proc. Natl. Acad. Sci. USA, 54, 1626–1632 (1965).
  • 14) Lin, T.-Y., Elbein, A. D., and Su, J.-C., Substrate specificity in pectin synthesis. Biochem. Biophys. Res. Commun., 22, 650–657 (1966).
  • 15) Bolwell, G. P., Dalessandro, G., and Northcote, D. H., Decrease of polygalacturonic acid synthase during xylem differentiation in sycamore. Phytochemistry, 24, 699–702 (1985).
  • 16) Doong, R. L., Liljebjelke, K., Fralish, G., Kumar, A., and Mohnen, D., Cell-free synthesis of pectin: identification and partial characterization of polygalacturonate 4-α-galacturonosyltransferase and its products from membrane preparations of tobacco cell suspension cultures. Plant Physiol., 109, 141–152 (1995).
  • 17) Doong, R. L., and Mohnen, D., Solubilization and characterization of a galacturosyltransferase that synthesizes the pectic polysaccharide homogalacturonan. Plant J., 13, 363–374 (1998).
  • 18) Akita, K., Ishimizu, T., Tsukamoto, T., Ando, T., and Hase, S., Successive glycosyltransfer activity and enzymatic characterization of pectic polygalacturonate 4-α-galacturonosyltransferase solubilized from pollen tubes of Petunia axillaris using pyridylaminated oligogalacturonates as substrates. Plant Physiol., 130, 374–379 (2002).
  • 19) Takeuchi, Y., and Tsumuraya, Y., In vitro biosynthesis of homogalacturonan by a membrane-bound galacturonosyltransferase from epicotyls of azuki bean. Biosci. Biotechnol. Biochem., 65, 1519–1527 (2001).
  • 20) Ishii, T., Ichita, J., Matsue, H., Ono, H., and Maeda, I., Fluorescent labeling of pectic oligosaccharides with 2-aminobenzamide and enzyme assay for pectin. Carbohydr. Res., 337, 1023–1032 (2002).
  • 21) Scheller, H. V., Doong, R. L., Ridley, B. L., and Mohnen, D., Pectin biosynthesis: a solubilized α1,4-galacturonosyltransferase from tobacco catalyzes the transfer of galacturonic acid from UDP-galacturonic acid onto the non-reducing end of homogalacturonan. Planta, 207, 512–517 (1999).
  • 22) Sterling, J. D., Quigley, H. F., Orellana, A., and Mohnen, D., The catalytic site of the pectin biosynthetic enzyme α-1,4-galacturonosyltransferase is located in the lumen of the Golgi. Plant Physiol., 127, 360–371 (2001).
  • 23) Perrin, R., Wilkerson, C., and Keegstra, K., Golgi enzymes that synthesize plant cell wall polysaccharides: finding and evaluating candidates in the genomic era. Plant Mol. Biol., 47, 115–130 (2001).
  • 24) Ohashi, T., Cramer, N., Ishimizu, T., and Hase, S., Preparation of UDP-galacturonic acid using UDP-sugar pyrophosphorylase. Anal. Biochem., 352, 182–188 (2006).
  • 25) Rheinberger, H. J., Geigenmuller, U., Wedde, M., and Nierhaus, K. H., Parameters for the preparation of Escherichia coli ribosomes and ribosomal subunits active in tRNA binding. Methods Enzymol., 164, 658–670 (1988).
  • 26) Ackers, G. K., A new calibration procedure for gel filtration columns. J. Biol. Chem., 242, 3237–3238 (1967).
  • 27) Luthe, D. S., A simple technique for the preparation and storage of sucrose gradients. Anal. Biochem., 135, 230–232 (1938).
  • 28) McEwen, C. R., Tables for estimating sedimentation through linear concentration gradients of sucrose solution. Anal. Biochem., 20, 114–149 (1967).
  • 29) Hammonds Jr., R. G., Nicolas, P., and Li, C. H., Characterization of β-endorphin binding protein (receptor) from rat brain membranes. Proc. Natl. Acad. Sci. USA, 79, 6494–6496 (1982).
  • 30) Horne, W. A., Weiland, G. A., and Oswald, R. E., Solubilization and hydrodynamic characterization of the dihydropyridine receptor from rat ventricular muscle. J. Biol. Chem., 261, 3588–3594 (1986).
  • 31) Rylett, R. J., Solubilization and partial characterization of [3H]choline mustard-labeled high-affinity choline carrier from presynaptic plasma membrane of Torpedo electric organ. J. Mol. Neurosci., 2, 85–90 (1990).
  • 32) Schwarzer, A., Kim, T. S. Y., Hagen, V., Molday, R. S., and Bauer, P. J., The Na/Ca-K exchanger of rod photoreceptor exists as dimer in the plasma membrane. Biochemistry, 36, 13667–13676 (1997).
  • 33) Clarke, S., The size and detergent binding of membrane proteins. J. Biol. Chem., 250, 5459–5469 (1975).
  • 34) Evans, H. J., and Sorger, G. J., Role of mineral elements with emphasis on the univalent cations. Annu. Rev. Plant Physiol., 17, 47–76 (1966).
  • 35) Goubet, F., Council, L. N., and Mohnen, D., Identification and partial characterization of the pectin methyltransferase “homogalacturonan-methyltransferase” from membrane of tobacco cell suspensions. Plant Physiol., 115, 337–347 (1998).
  • 36) Orlow, S. J., Zhou, B.-K., Chakraborty, A. K., Drucker, M., Pifko-Hirst, S., and Pawelek, J. M., High-molecular-weight forms of tyrosinase and the tyrosinase-related proteins: evidence for a melanogenic complex. J. Invest. Dermatol., 103, 196–201 (1994).
  • 37) Kanayama, H., Tamura, T., Ugai, S., Kagawa, S., Tanahashi, N., Yoshimura, T., Tanaka, K., and Ichihara, A., Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur. J. Biochem., 206, 567–578 (1992).
  • 38) Kauss, H., and Swanson, A. L., Cooperation of enzymes responsible for polymerisation and methylation in pectin biosynthesis. Z. Naturforschg., 24b, 28–33 (1969).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.