Abstract
A study of the degradation of plant cell walls by the mixture of enzymes present in Pectinol R-10 is described. A “wall-modifying enzyme” has been purified from this mixture by a combination of diethylaminoethyl cellulose, Bio Gel P-100, and carboxymethyl cellulose chromatography. Treatment of cell walls with the “wall-modifying enzyme” is shown to be a necessary prerequisite to wall degradation catalyzed by a mixture of polysaccharide-degrading enzymes prepared from Pectinol R-10 or by an α-galactosidase secreted by the pathogenic fungus Colletotrichum lindemuthianum. The action of the “wall-modifying enzyme” on cell walls is shown to result in both a release of water-soluble, 70% ethanol-insoluble polymers and an alteration of the residual cell wall. A purified preparation of the “wall-modifying enzyme” is unable to degrade a wide variety of polysaccharide, glycoside, and peptide substrates. However, the purified preparation of wall-modifying enzyme has a limited ability to degrade polygalacturonic acid. The fact that polygalacturonic acid inhibits the ability of the “wall-modifying enzyme” to affect cell walls suggests that the “wall-modifying enzyme” may be responsible for the limited polygalacturonic acid-degrading activity present in the purified preparation. The importance of a wall-modifying enzyme in developmental processes and in pathogenesis is discussed.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALBERSHEIM P., KILLIAS U. Studies relating to the purification and properties of pectin transeliminase. Arch Biochem Biophys. 1962 Apr;97:107–115. doi: 10.1016/0003-9861(62)90050-4. [DOI] [PubMed] [Google Scholar]
- Abeles F. B. Abscission: role of cellulase. Plant Physiol. 1969 Mar;44(3):447–452. doi: 10.1104/pp.44.3.447. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Agrawal K. M., Bahl O. P. Glycosidases of Phaseolus vulgaris. II. Isolation and general properties. J Biol Chem. 1968 Jan 10;243(1):103–111. [PubMed] [Google Scholar]
- BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
- Bailey P. J., Liese W., Roesch R., Keilich G., Afting E. G. Cellulase (beta-1,4-glucan 4-glucanohydrolase) from the wood-degrading fungus Polyporus schweinitzii Fr. I. Purification. Biochim Biophys Acta. 1969;185(2):381–391. doi: 10.1016/0005-2744(69)90431-8. [DOI] [PubMed] [Google Scholar]
- Bateman D. F., Van Etten H. D. Susceptibility to Enzymatic Degradation of Cell Walls From Bean Plants Resistant and Susceptible to Rhizoctonia solani Kuhn. Plant Physiol. 1969 May;44(5):641–648. doi: 10.1104/pp.44.5.641. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cleland R. Hydroxyproline Formation and Its Relation to Auxin-induced Cell Elongation in the Avena Coleoptile. Plant Physiol. 1968 Oct;43(10):1625–1630. doi: 10.1104/pp.43.10.1625. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Datko A. H., Maclachlan G. A. Indoleacetic Acid and the synthesis of glucanases and pectic enzymes. Plant Physiol. 1968 May;43(5):735–742. doi: 10.1104/pp.43.5.735. [DOI] [PMC free article] [PubMed] [Google Scholar]
- English P. D., Albersheim P. Host-Pathogen Interactions: I. A Correlation Between alpha-Galactosidase Production and Virulence. Plant Physiol. 1969 Feb;44(2):217–224. doi: 10.1104/pp.44.2.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Evans M. L., Ray P. M. Timing of the auxin response in coleoptiles and its implications regarding auxin action. J Gen Physiol. 1969 Jan;53(1):1–20. doi: 10.1085/jgp.53.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GREEN M. N., TSOU K. C., BRESSLER R., SELIGMAN A. M. The colorimetric determination of leucine aminopeptidase activity with L-leucyl-beta-naphthylamide hydrochloride. Arch Biochem Biophys. 1955 Aug;57(2):458–474. doi: 10.1016/0003-9861(55)90307-6. [DOI] [PubMed] [Google Scholar]
- Ghuysen J. M. Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol Rev. 1968 Dec;32(4 Pt 2):425–464. [PMC free article] [PubMed] [Google Scholar]
- Keilich G., Bailey P. J., Afting E. G., Liese W. Cellulase (beta-1,4-glucan 4-glucanohydrolase) from the wood-degrading fungus Polyporus schweinitzii Fr. II. Characterization. Biochim Biophys Acta. 1969;185(2):392–401. doi: 10.1016/0005-2744(69)90432-x. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- 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]
- Lee M., Macmillan J. D. Mode of action of pectic enzymes. I. Purification and certain properties of tomato pectinesterase. Biochemistry. 1968 Nov;7(11):4005–4010. doi: 10.1021/bi00851a030. [DOI] [PubMed] [Google Scholar]
- Lee S. H., Kivilaan A., Bandurski R. S. In vitro autolysis of plant cell walls. Plant Physiol. 1967 Jul;42(7):968–972. doi: 10.1104/pp.42.7.968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morre D. J. Cell wall dissolution and enzyme secretion during leaf abscission. Plant Physiol. 1968 Sep;43(9 Pt B):1545–1559. [PMC free article] [PubMed] [Google Scholar]
- REESE E. T., SIU R. G. H., LEVINSON H. S. The biological degradation of soluble cellulose derivatives and its relationship to the mechanism of cellulose hydrolysis. J Bacteriol. 1950 Apr;59(4):485–497. doi: 10.1128/jb.59.4.485-497.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SCHWERT G. W., TAKENAKA Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta. 1955 Apr;16(4):570–575. doi: 10.1016/0006-3002(55)90280-8. [DOI] [PubMed] [Google Scholar]
- Selby K., Maitland C. C. The cellulase of Trichoderma viride. Separation of the components involved in the solubilization of cotton. Biochem J. 1967 Sep;104(3):716–724. doi: 10.1042/bj1040716. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stowe B. B., Obreiter J. B. Growth Promotion in Pea Stem Sections. II. By Natural Oils & Isoprenoid Vitamins. Plant Physiol. 1962 Mar;37(2):158–164. doi: 10.1104/pp.37.2.158. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Strominger J. L., Ghuysen J. M. Mechanisms of enzymatic bacteriaolysis. Cell walls of bacteri are solubilized by action of either specific carbohydrases or specific peptidases. Science. 1967 Apr 14;156(3772):213–221. doi: 10.1126/science.156.3772.213. [DOI] [PubMed] [Google Scholar]
- YACHNIN S. Non-antigenicity of synthetic polyribonucleotides and apurinic acid. Nature. 1962 Sep 29;195:1319–1319. doi: 10.1038/1951319a0. [DOI] [PubMed] [Google Scholar]
- Yager R. E. Possible Role of Pectic Enzymes in Abscission. Plant Physiol. 1960 Mar;35(2):157–162. doi: 10.1104/pp.35.2.157. [DOI] [PMC free article] [PubMed] [Google Scholar]