Recombinant production of membrane proteins in yeast

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

Standard

Recombinant production of membrane proteins in yeast. / Preisler, Sarah Spruce; Hansen, Karen Molbæk; Nurup, Casper Normann; Beich-Frandsen, Mads; Pedersen, Per Amstrup.

Methods in Enzymology. ed. / Anna Marie Pyle; David W. Christianson. Vol. 660 Academic Press, 2021. p. 21-52 (Methods in Enzymology, Vol. 660).

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

Harvard

Preisler, SS, Hansen, KM, Nurup, CN, Beich-Frandsen, M & Pedersen, PA 2021, Recombinant production of membrane proteins in yeast. in AM Pyle & DW Christianson (eds), Methods in Enzymology. vol. 660, Academic Press, Methods in Enzymology, vol. 660, pp. 21-52. https://doi.org/10.1016/bs.mie.2021.07.003

APA

Preisler, S. S., Hansen, K. M., Nurup, C. N., Beich-Frandsen, M., & Pedersen, P. A. (2021). Recombinant production of membrane proteins in yeast. In A. M. Pyle, & D. W. Christianson (Eds.), Methods in Enzymology (Vol. 660, pp. 21-52). Academic Press. Methods in Enzymology Vol. 660 https://doi.org/10.1016/bs.mie.2021.07.003

Vancouver

Preisler SS, Hansen KM, Nurup CN, Beich-Frandsen M, Pedersen PA. Recombinant production of membrane proteins in yeast. In Pyle AM, Christianson DW, editors, Methods in Enzymology. Vol. 660. Academic Press. 2021. p. 21-52. (Methods in Enzymology, Vol. 660). https://doi.org/10.1016/bs.mie.2021.07.003

Author

Preisler, Sarah Spruce ; Hansen, Karen Molbæk ; Nurup, Casper Normann ; Beich-Frandsen, Mads ; Pedersen, Per Amstrup. / Recombinant production of membrane proteins in yeast. Methods in Enzymology. editor / Anna Marie Pyle ; David W. Christianson. Vol. 660 Academic Press, 2021. pp. 21-52 (Methods in Enzymology, Vol. 660).

Bibtex

@inbook{9a73433cf6904e089470ac4b65eb7b95,

title = "Recombinant production of membrane proteins in yeast",

abstract = "Biochemical pathways are compartmentalized in living cells. This permits each cell to maintain chemical compositions that differ between the cytosol, intracellular organelles and the external environment. Achieving this requires each compartment to be very selective in what is allowed to enter and leave. Nature has solved this by surrounding each cell and each organelle with a virtually solute impermeable lipid membrane, embedded with integral membrane proteins that mediate strictly controlled trans-membrane movement of matter and information. Access to pure and active integral membrane proteins is therefore required to comprehend membrane biology, ultimately through high-resolution structures of the membrane proteome and, therefore, also for our understanding of physiology. Unfortunately, apart from a few exceptions, membrane proteins cannot be purified from native tissue but need to be produced recombinantly, which is eminently challenging. This chapter shows how we have engineered yeast to provide high levels of prime quality membrane proteins of prokaryotic, archaeal or eukaryotic origin for structural biology.",

keywords = "Heterologous proteins, Membrane proteins, Structural biology",

author = "Preisler, {Sarah Spruce} and Hansen, {Karen Molb{\ae}k} and Nurup, {Casper Normann} and Mads Beich-Frandsen and Pedersen, {Per Amstrup}",

note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Inc.",

year = "2021",

doi = "10.1016/bs.mie.2021.07.003",

language = "English",

isbn = "978-0-323-90737-8",

volume = "660",

series = "Methods in Enzymology",

pages = "21--52",

editor = "Pyle, {Anna Marie} and Christianson, {David W.}",

booktitle = "Methods in Enzymology",

publisher = "Academic Press",

address = "United States",

}

RIS

TY - CHAP

T1 - Recombinant production of membrane proteins in yeast

AU - Preisler, Sarah Spruce

AU - Hansen, Karen Molbæk

AU - Nurup, Casper Normann

AU - Beich-Frandsen, Mads

AU - Pedersen, Per Amstrup

PY - 2021

Y1 - 2021

N2 - Biochemical pathways are compartmentalized in living cells. This permits each cell to maintain chemical compositions that differ between the cytosol, intracellular organelles and the external environment. Achieving this requires each compartment to be very selective in what is allowed to enter and leave. Nature has solved this by surrounding each cell and each organelle with a virtually solute impermeable lipid membrane, embedded with integral membrane proteins that mediate strictly controlled trans-membrane movement of matter and information. Access to pure and active integral membrane proteins is therefore required to comprehend membrane biology, ultimately through high-resolution structures of the membrane proteome and, therefore, also for our understanding of physiology. Unfortunately, apart from a few exceptions, membrane proteins cannot be purified from native tissue but need to be produced recombinantly, which is eminently challenging. This chapter shows how we have engineered yeast to provide high levels of prime quality membrane proteins of prokaryotic, archaeal or eukaryotic origin for structural biology.

AB - Biochemical pathways are compartmentalized in living cells. This permits each cell to maintain chemical compositions that differ between the cytosol, intracellular organelles and the external environment. Achieving this requires each compartment to be very selective in what is allowed to enter and leave. Nature has solved this by surrounding each cell and each organelle with a virtually solute impermeable lipid membrane, embedded with integral membrane proteins that mediate strictly controlled trans-membrane movement of matter and information. Access to pure and active integral membrane proteins is therefore required to comprehend membrane biology, ultimately through high-resolution structures of the membrane proteome and, therefore, also for our understanding of physiology. Unfortunately, apart from a few exceptions, membrane proteins cannot be purified from native tissue but need to be produced recombinantly, which is eminently challenging. This chapter shows how we have engineered yeast to provide high levels of prime quality membrane proteins of prokaryotic, archaeal or eukaryotic origin for structural biology.

KW - Heterologous proteins

KW - Membrane proteins

KW - Structural biology

U2 - 10.1016/bs.mie.2021.07.003

DO - 10.1016/bs.mie.2021.07.003

M3 - Book chapter

C2 - 34742390

AN - SCOPUS:85112844498

SN - 978-0-323-90737-8

VL - 660

T3 - Methods in Enzymology

SP - 21

EP - 52

BT - Methods in Enzymology

A2 - Pyle, Anna Marie

A2 - Christianson, David W.

PB - Academic Press

ER -

ID: 281280938

Department of Biology