Molecular snapshots of dynamic membrane-bound metabolons

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Molecular snapshots of dynamic membrane-bound metabolons. / Bassard, Jean Etienne; Laursen, Tomas.

Methods in Enzymology. Vol. 617 Academic Press, 2019. p. 1-27 (Methods in Enzymology, Vol. 617).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Bassard, JE & Laursen, T 2019, Molecular snapshots of dynamic membrane-bound metabolons. in Methods in Enzymology. vol. 617, Academic Press, Methods in Enzymology, vol. 617, pp. 1-27. https://doi.org/10.1016/bs.mie.2018.12.001

APA

Bassard, J. E., & Laursen, T. (2019). Molecular snapshots of dynamic membrane-bound metabolons. In Methods in Enzymology (Vol. 617, pp. 1-27). Academic Press. Methods in Enzymology Vol. 617 https://doi.org/10.1016/bs.mie.2018.12.001

Vancouver

Bassard JE, Laursen T. Molecular snapshots of dynamic membrane-bound metabolons. In Methods in Enzymology. Vol. 617. Academic Press. 2019. p. 1-27. (Methods in Enzymology, Vol. 617). https://doi.org/10.1016/bs.mie.2018.12.001

Author

Bassard, Jean Etienne ; Laursen, Tomas. / Molecular snapshots of dynamic membrane-bound metabolons. Methods in Enzymology. Vol. 617 Academic Press, 2019. pp. 1-27 (Methods in Enzymology, Vol. 617).

Bibtex

@inbook{20101337287849be8d85819aba339bb8,
title = "Molecular snapshots of dynamic membrane-bound metabolons",
abstract = "Numerous biosynthetic pathways have been shown to assemble at the surface of cellular membranes into efficient dynamic supramolecular assemblies termed metabolons. In response to environmental stimuli, metabolons assemble on-demand making them highly dynamic and fragile. This transient nature has previously hampered isolation and molecular characterization of dynamic metabolons. In contrast to conventional detergents, which tend to disrupt weak protein–protein interactions and remove lipids, the competence of a styrene maleic acid copolymer to carve out discrete lipid nanodisc from membranes offers immense potential for isolation of intact protein assemblies. Here, we present a method to extract the entire membrane-bound dhurrin pathway directly from microsomal fractions of the cereal Sorghum bicolor. This detergent-free nanodisc approach may be generally transposed for isolation of entire plant biosynthetic metabolons. This method provides a simple practical toolkit for the study of membrane protein complexes.",
keywords = "Cytochromes P450, Detergent free, Dhurrin metabolon, Metabolon, Metabolon isolation, Microsome preparation, NADPH-dependent cytochrome P450 oxidoreductase, Styrene maleic acid copolymer, Styrene maleic acid lipid particles",
author = "Bassard, {Jean Etienne} and Tomas Laursen",
year = "2019",
month = jan,
day = "1",
doi = "10.1016/bs.mie.2018.12.001",
language = "English",
volume = "617",
series = "Methods in Enzymology",
publisher = "Academic Press",
pages = "1--27",
booktitle = "Methods in Enzymology",
address = "United States",

}

RIS

TY - CHAP

T1 - Molecular snapshots of dynamic membrane-bound metabolons

AU - Bassard, Jean Etienne

AU - Laursen, Tomas

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Numerous biosynthetic pathways have been shown to assemble at the surface of cellular membranes into efficient dynamic supramolecular assemblies termed metabolons. In response to environmental stimuli, metabolons assemble on-demand making them highly dynamic and fragile. This transient nature has previously hampered isolation and molecular characterization of dynamic metabolons. In contrast to conventional detergents, which tend to disrupt weak protein–protein interactions and remove lipids, the competence of a styrene maleic acid copolymer to carve out discrete lipid nanodisc from membranes offers immense potential for isolation of intact protein assemblies. Here, we present a method to extract the entire membrane-bound dhurrin pathway directly from microsomal fractions of the cereal Sorghum bicolor. This detergent-free nanodisc approach may be generally transposed for isolation of entire plant biosynthetic metabolons. This method provides a simple practical toolkit for the study of membrane protein complexes.

AB - Numerous biosynthetic pathways have been shown to assemble at the surface of cellular membranes into efficient dynamic supramolecular assemblies termed metabolons. In response to environmental stimuli, metabolons assemble on-demand making them highly dynamic and fragile. This transient nature has previously hampered isolation and molecular characterization of dynamic metabolons. In contrast to conventional detergents, which tend to disrupt weak protein–protein interactions and remove lipids, the competence of a styrene maleic acid copolymer to carve out discrete lipid nanodisc from membranes offers immense potential for isolation of intact protein assemblies. Here, we present a method to extract the entire membrane-bound dhurrin pathway directly from microsomal fractions of the cereal Sorghum bicolor. This detergent-free nanodisc approach may be generally transposed for isolation of entire plant biosynthetic metabolons. This method provides a simple practical toolkit for the study of membrane protein complexes.

KW - Cytochromes P450

KW - Detergent free

KW - Dhurrin metabolon

KW - Metabolon

KW - Metabolon isolation

KW - Microsome preparation

KW - NADPH-dependent cytochrome P450 oxidoreductase

KW - Styrene maleic acid copolymer

KW - Styrene maleic acid lipid particles

UR - http://www.scopus.com/inward/record.url?scp=85060301531&partnerID=8YFLogxK

U2 - 10.1016/bs.mie.2018.12.001

DO - 10.1016/bs.mie.2018.12.001

M3 - Book chapter

C2 - 30784399

AN - SCOPUS:85060301531

VL - 617

T3 - Methods in Enzymology

SP - 1

EP - 27

BT - Methods in Enzymology

PB - Academic Press

ER -

ID: 216212893