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Tania Aaquist Ammitzbøll

Secreted major Venus flytrap chitinase enables digestion of Arthropod prey

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Secreted major Venus flytrap chitinase enables digestion of Arthropod prey. / Paszota, Paulina; Escalante-Perez, Maria; Thomsen, Line R; Risør, Michael Wulff; Dembski, Alicja; Sanglas, Laura ; Nielsen, Tania A; Karring, Henrik; Thøgersen, Ida B; Hedrich, Rainer; Enghild, Jan Johannes; Kreuzer, Ines; Sanggaard, Kristian W.

In: BBA General Subjects, Vol. 1844, No. 2, 02.2014, p. 374–383.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Paszota, P, Escalante-Perez, M, Thomsen, LR, Risør, MW, Dembski, A, Sanglas, L, Nielsen, TA, Karring, H, Thøgersen, IB, Hedrich, R, Enghild, JJ, Kreuzer, I & Sanggaard, KW 2014, 'Secreted major Venus flytrap chitinase enables digestion of Arthropod prey', BBA General Subjects, vol. 1844, no. 2, pp. 374–383. https://doi.org/10.1016/j.bbapap.2013.11.009

APA

Paszota, P., Escalante-Perez, M., Thomsen, L. R., Risør, M. W., Dembski, A., Sanglas, L., Nielsen, T. A., Karring, H., Thøgersen, I. B., Hedrich, R., Enghild, J. J., Kreuzer, I., & Sanggaard, K. W. (2014). Secreted major Venus flytrap chitinase enables digestion of Arthropod prey. BBA General Subjects, 1844(2), 374–383. https://doi.org/10.1016/j.bbapap.2013.11.009

CBE

Paszota P, Escalante-Perez M, Thomsen LR, Risør MW, Dembski A, Sanglas L, Nielsen TA, Karring H, Thøgersen IB, Hedrich R, Enghild JJ, Kreuzer I, Sanggaard KW. 2014. Secreted major Venus flytrap chitinase enables digestion of Arthropod prey. BBA General Subjects. 1844(2):374–383. https://doi.org/10.1016/j.bbapap.2013.11.009

MLA

Vancouver

Paszota P, Escalante-Perez M, Thomsen LR, Risør MW, Dembski A, Sanglas L et al. Secreted major Venus flytrap chitinase enables digestion of Arthropod prey. BBA General Subjects. 2014 Feb;1844(2):374–383. https://doi.org/10.1016/j.bbapap.2013.11.009

Author

Paszota, Paulina ; Escalante-Perez, Maria ; Thomsen, Line R ; Risør, Michael Wulff ; Dembski, Alicja ; Sanglas, Laura ; Nielsen, Tania A ; Karring, Henrik ; Thøgersen, Ida B ; Hedrich, Rainer ; Enghild, Jan Johannes ; Kreuzer, Ines ; Sanggaard, Kristian W. / Secreted major Venus flytrap chitinase enables digestion of Arthropod prey. In: BBA General Subjects. 2014 ; Vol. 1844, No. 2. pp. 374–383.

Bibtex

@article{3cb641fe0bd142e9946cf1ae4b16a907,
title = "Secreted major Venus flytrap chitinase enables digestion of Arthropod prey",
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 α-chitin.",
keywords = "Carnivorous plants, Plant biology, Digestive enzymes, Chitin, Chitinases",
author = "Paulina Paszota and Maria Escalante-Perez and Thomsen, {Line R} and Ris{\o}r, {Michael Wulff} and Alicja Dembski and Laura Sanglas and Nielsen, {Tania A} and Henrik Karring and Th{\o}gersen, {Ida B} and Rainer Hedrich and Enghild, {Jan Johannes} and Ines Kreuzer and Sanggaard, {Kristian W}",
note = "Copyright {\textcopyright} 2013. Published by Elsevier B.V.",
year = "2014",
month = feb,
doi = "10.1016/j.bbapap.2013.11.009",
language = "English",
volume = "1844",
pages = "374–383",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier BV",
number = "2",

}

RIS

TY - JOUR

T1 - Secreted major Venus flytrap chitinase enables digestion of Arthropod prey

AU - Paszota, Paulina

AU - Escalante-Perez, Maria

AU - Thomsen, Line R

AU - Risør, Michael Wulff

AU - Dembski, Alicja

AU - Sanglas, Laura

AU - Nielsen, Tania A

AU - Karring, Henrik

AU - Thøgersen, Ida B

AU - Hedrich, Rainer

AU - Enghild, Jan Johannes

AU - Kreuzer, Ines

AU - Sanggaard, Kristian W

N1 - Copyright © 2013. Published by Elsevier B.V.

PY - 2014/2

Y1 - 2014/2

N2 - 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 α-chitin.

AB - 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 α-chitin.

KW - Carnivorous plants

KW - Plant biology

KW - Digestive enzymes

KW - Chitin

KW - Chitinases

U2 - 10.1016/j.bbapap.2013.11.009

DO - 10.1016/j.bbapap.2013.11.009

M3 - Journal article

C2 - 24275507

VL - 1844

SP - 374

EP - 383

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -