%0 Journal Article %1 RN1072 %A Paszota, P. %A Escalante-Perez, M. %A Thomsen, L. R. %A Risor, M. W. %A Dembski, A. %A Sanglas, L. %A Nielsen, T. A. %A Karring, H. %A Thogersen, I. B. %A Hedrich, R. %A Enghild, J. J. %A Kreuzer, I. %A Sanggaard, K. W. %D 2014 %J Biochimica Et Biophysica Acta-Proteins and Proteomics %K carnivorous myOwn plants %N 2 %P 374-383 %R 10.1016/j.bbapap.2013.11.009 %T Secreted major Venus flytrap chitinase enables digestion of Arthropod prey %U /brokenurl#<Go to ISI>://WOS:000330489000010 %V 1844 %X Predation plays a major role in energy and nutrient flow in the biological food chain. Plant carnivory has attracted much interest since Darwin's time, but many fundamental properties of the carnivorous lifestyle are largely unexplored. In particular, the chain of events leading from prey perception to its digestive utilization remains to be elucidated. One of the first steps after the capture of animal prey, i.e. the enzymatic breakup of the insects' chitin-based shell, is reflected by considerable chitinase activity in the secreted digestive fluid in the carnivorous plant Venus flytrap. This study addresses the molecular nature, function, and regulation of the underlying enzyme, VF chitinase-I. Using mass spectrometry based de novo sequencing, VF chitinase-I was identified in the secreted fluid. As anticipated for one of the most prominent proteins in the flytrap's "green stomach" during prey digestion, transcription of VF chitinase-I is restricted to glands and enhanced by secretion-inducing stimuli. In their natural habitat, Venus flytrap is exposed to high temperatures. We expressed and purified recombinant VF chitinase-I and show that the enzyme exhibits the hallmark properties expected from an enzyme active in the hot and acidic digestive fluid of Dionaea muscipula. Structural modeling revealed a relative compact globular form of VF chitinase-I, which might contribute to its overall stability and resistance to proteolysis. These peculiar characteristics could well serve industrial purposes, especially because of the ability to hydrolyze both soluble and crystalline chitin substrates including the commercially important cleavage of alpha-chitin. (C) 2013 Elsevier B.V. All rights reserved.

@article{RN1072, abstract = {Predation plays a major role in energy and nutrient flow in the biological food chain. Plant carnivory has attracted much interest since Darwin's time, but many fundamental properties of the carnivorous lifestyle are largely unexplored. In particular, the chain of events leading from prey perception to its digestive utilization remains to be elucidated. One of the first steps after the capture of animal prey, i.e. the enzymatic breakup of the insects' chitin-based shell, is reflected by considerable chitinase activity in the secreted digestive fluid in the carnivorous plant Venus flytrap. This study addresses the molecular nature, function, and regulation of the underlying enzyme, VF chitinase-I. Using mass spectrometry based de novo sequencing, VF chitinase-I was identified in the secreted fluid. As anticipated for one of the most prominent proteins in the flytrap's "green stomach" during prey digestion, transcription of VF chitinase-I is restricted to glands and enhanced by secretion-inducing stimuli. In their natural habitat, Venus flytrap is exposed to high temperatures. We expressed and purified recombinant VF chitinase-I and show that the enzyme exhibits the hallmark properties expected from an enzyme active in the hot and acidic digestive fluid of Dionaea muscipula. Structural modeling revealed a relative compact globular form of VF chitinase-I, which might contribute to its overall stability and resistance to proteolysis. These peculiar characteristics could well serve industrial purposes, especially because of the ability to hydrolyze both soluble and crystalline chitin substrates including the commercially important cleavage of alpha-chitin. (C) 2013 Elsevier B.V. All rights reserved.}, added-at = {2024-02-14T14:38:32.000+0100}, author = {Paszota, P. and Escalante-Perez, M. and Thomsen, L. R. and Risor, M. W. and Dembski, A. and Sanglas, L. and Nielsen, T. A. and Karring, H. and Thogersen, I. B. and Hedrich, R. and Enghild, J. J. and Kreuzer, I. and Sanggaard, K. W.}, biburl = {https://www.bibsonomy.org/bibtex/2366be833ccc5248a396969176b111c90/rainerhedrich_2}, doi = {10.1016/j.bbapap.2013.11.009}, interhash = {00fd90e11a8d4cdd3d5829d501c848be}, intrahash = {366be833ccc5248a396969176b111c90}, issn = {1570-9639}, journal = {Biochimica Et Biophysica Acta-Proteins and Proteomics}, keywords = {carnivorous myOwn plants}, note = {300uh Times Cited:35 Cited References Count:73}, number = 2, pages = {374-383}, timestamp = {2024-02-14T14:38:32.000+0100}, title = {Secreted major Venus flytrap chitinase enables digestion of Arthropod prey}, type = {Journal Article}, url = {/brokenurl#<Go to ISI>://WOS:000330489000010}, volume = 1844, year = 2014 }