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Ethylene Biosynthesis-Inducing Xylanase II. Purification and Physical Characterization of the Enzyme Produced by Trichoderma viride

Ethylene Biosynthesis-Inducing Xylanase II. Purification and Physical Characterization of the... Abstract The ethylene biosynthesis-inducing endoxylanase (EIX) from xylan-induced cultures of the fungus, Trichoderma viride, was purified to near homogeneity and compared with the EIX isolated from Cellulysin. Both enzymes migrate as 9.2 kilodalton proteins during gel filtration chromatography under nondenaturing conditions, but the mature polypeptide migrates as a 22 kilodalton band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition of the 22 kilodalton polypeptide is enriched by Gly, Ser, Thr, Trp, and Tyr, but depleted in Ala, Glx, Leu, and Lys. Both proteins lack sulfur-containing amino acids. The protein is glycosylated, and inhibition of EIX synthesis by tunicamycin suggests that at least some of the sugar moieties are linked to asparagine residues. EIX appears to be synthesized initially as a 25 kilodalton precursor protein that is processed to 22 kilodalton during secretion. 2 Current address: Center for Biological Resource Recovery, Department of Biochemistry, University of Georgia, Athens, GA 30605. 1 This work was supported, in part, by grant I-1165-86 from the U.S.-Israel Binational Agricultural Research and Development Fund and by U.S. Department of Agriculture Competitive grant No. 88-37261-3680 to J. D. A. and J. F. D. D. This content is only available as a PDF. © 1991 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Physiology Oxford University Press

Ethylene Biosynthesis-Inducing Xylanase II. Purification and Physical Characterization of the Enzyme Produced by Trichoderma viride

Dean, Jeffrey F. D.; Anderson, J. D.
Plant Physiology , Volume 95 (1) – Jan 1, 1991
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References (35)

Publisher
Oxford University Press
Copyright
Copyright © 2021 American Society of Plant Biologists
ISSN
0032-0889
eISSN
1532-2548
DOI
10.1104/pp.95.1.316
Publisher site
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Abstract

Abstract The ethylene biosynthesis-inducing endoxylanase (EIX) from xylan-induced cultures of the fungus, Trichoderma viride, was purified to near homogeneity and compared with the EIX isolated from Cellulysin. Both enzymes migrate as 9.2 kilodalton proteins during gel filtration chromatography under nondenaturing conditions, but the mature polypeptide migrates as a 22 kilodalton band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition of the 22 kilodalton polypeptide is enriched by Gly, Ser, Thr, Trp, and Tyr, but depleted in Ala, Glx, Leu, and Lys. Both proteins lack sulfur-containing amino acids. The protein is glycosylated, and inhibition of EIX synthesis by tunicamycin suggests that at least some of the sugar moieties are linked to asparagine residues. EIX appears to be synthesized initially as a 25 kilodalton precursor protein that is processed to 22 kilodalton during secretion. 2 Current address: Center for Biological Resource Recovery, Department of Biochemistry, University of Georgia, Athens, GA 30605. 1 This work was supported, in part, by grant I-1165-86 from the U.S.-Israel Binational Agricultural Research and Development Fund and by U.S. Department of Agriculture Competitive grant No. 88-37261-3680 to J. D. A. and J. F. D. D. This content is only available as a PDF. © 1991 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Journal

Plant Physiology – Oxford University Press

Published: Jan 1, 1991

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