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The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms

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Standard

The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. / Schulze, Waltraud X; Sanggaard, Kristian Wejse; Kreuzer, Ines; Knudsen, Anders D; Bemm, Felix; Thøgersen, Ida B; Brautigam, Andrea; Thomsen, Line R; Schliesky, Simon; Dyrlund, Thomas Franck; Escalante-Perez, Maria; Becker, Dirk; Schultz, Jörg; Karring, Henrik; Weber, Andreas; Højrup, Peter; Hedrich, Rainer; Enghild, Jan Johannes.

In: Molecular and Cellular Proteomics, Vol. 11, No. 11, 01.11.2012, p. 1306-1319.

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

Harvard

Schulze, WX, Sanggaard, KW, Kreuzer, I, Knudsen, AD, Bemm, F, Thøgersen, IB, Brautigam, A, Thomsen, LR, Schliesky, S, Dyrlund, TF, Escalante-Perez, M, Becker, D, Schultz, J, Karring, H, Weber, A, Højrup, P, Hedrich, R & Enghild, JJ 2012, 'The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms', Molecular and Cellular Proteomics, vol. 11, no. 11, pp. 1306-1319. https://doi.org/10.1074/mcp.M112.021006

APA

Schulze, W. X., Sanggaard, K. W., Kreuzer, I., Knudsen, A. D., Bemm, F., Thøgersen, I. B., Brautigam, A., Thomsen, L. R., Schliesky, S., Dyrlund, T. F., Escalante-Perez, M., Becker, D., Schultz, J., Karring, H., Weber, A., Højrup, P., Hedrich, R., & Enghild, J. J. (2012). The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. Molecular and Cellular Proteomics, 11(11), 1306-1319. https://doi.org/10.1074/mcp.M112.021006

CBE

Schulze WX, Sanggaard KW, Kreuzer I, Knudsen AD, Bemm F, Thøgersen IB, Brautigam A, Thomsen LR, Schliesky S, Dyrlund TF, Escalante-Perez M, Becker D, Schultz J, Karring H, Weber A, Højrup P, Hedrich R, Enghild JJ. 2012. The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. Molecular and Cellular Proteomics. 11(11):1306-1319. https://doi.org/10.1074/mcp.M112.021006

MLA

Vancouver

Schulze WX, Sanggaard KW, Kreuzer I, Knudsen AD, Bemm F, Thøgersen IB et al. The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. Molecular and Cellular Proteomics. 2012 Nov 1;11(11):1306-1319. https://doi.org/10.1074/mcp.M112.021006

Author

Schulze, Waltraud X ; Sanggaard, Kristian Wejse ; Kreuzer, Ines ; Knudsen, Anders D ; Bemm, Felix ; Thøgersen, Ida B ; Brautigam, Andrea ; Thomsen, Line R ; Schliesky, Simon ; Dyrlund, Thomas Franck ; Escalante-Perez, Maria ; Becker, Dirk ; Schultz, Jörg ; Karring, Henrik ; Weber, Andreas ; Højrup, Peter ; Hedrich, Rainer ; Enghild, Jan Johannes. / The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms. In: Molecular and Cellular Proteomics. 2012 ; Vol. 11, No. 11. pp. 1306-1319.

Bibtex

@article{82a9006ac87f4bfe91606495a1e186ef,
title = "The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms",
abstract = "The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested to assimilate nutrients as the plants grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plant's digestive system evolved from defense-related processes. This in-depth characterization of a highly specialized secreted fluid from a carnivorous plant provides new information about its prey digestion mechanism and the evolutionary processes driving its defense pathways and nutrient acquisition.",
author = "Schulze, {Waltraud X} and Sanggaard, {Kristian Wejse} and Ines Kreuzer and Knudsen, {Anders D} and Felix Bemm and Th{\o}gersen, {Ida B} and Andrea Brautigam and Thomsen, {Line R} and Simon Schliesky and Dyrlund, {Thomas Franck} and Maria Escalante-Perez and Dirk Becker and J{\"o}rg Schultz and Henrik Karring and Andreas Weber and Peter H{\o}jrup and Rainer Hedrich and Enghild, {Jan Johannes}",
year = "2012",
month = nov,
day = "1",
doi = "10.1074/mcp.M112.021006",
language = "English",
volume = "11",
pages = "1306--1319",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology",
number = "11",

}

RIS

TY - JOUR

T1 - The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms

AU - Schulze, Waltraud X

AU - Sanggaard, Kristian Wejse

AU - Kreuzer, Ines

AU - Knudsen, Anders D

AU - Bemm, Felix

AU - Thøgersen, Ida B

AU - Brautigam, Andrea

AU - Thomsen, Line R

AU - Schliesky, Simon

AU - Dyrlund, Thomas Franck

AU - Escalante-Perez, Maria

AU - Becker, Dirk

AU - Schultz, Jörg

AU - Karring, Henrik

AU - Weber, Andreas

AU - Højrup, Peter

AU - Hedrich, Rainer

AU - Enghild, Jan Johannes

PY - 2012/11/1

Y1 - 2012/11/1

N2 - The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested to assimilate nutrients as the plants grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plant's digestive system evolved from defense-related processes. This in-depth characterization of a highly specialized secreted fluid from a carnivorous plant provides new information about its prey digestion mechanism and the evolutionary processes driving its defense pathways and nutrient acquisition.

AB - The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested to assimilate nutrients as the plants grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plant's digestive system evolved from defense-related processes. This in-depth characterization of a highly specialized secreted fluid from a carnivorous plant provides new information about its prey digestion mechanism and the evolutionary processes driving its defense pathways and nutrient acquisition.

U2 - 10.1074/mcp.M112.021006

DO - 10.1074/mcp.M112.021006

M3 - Journal article

C2 - 22891002

VL - 11

SP - 1306

EP - 1319

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 11

ER -