Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A. / Behrendorff, James B Y H; Sandoval-Ibañez, Omar A; Sharma, Anurag; Pribil, Mathias.

In: A C S Synthetic Biology, Vol. 8, No. 4, 19.04.2019, p. 611-620.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Behrendorff, JBYH, Sandoval-Ibañez, OA, Sharma, A & Pribil, M 2019, 'Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A', A C S Synthetic Biology, vol. 8, no. 4, pp. 611-620. https://doi.org/10.1021/acssynbio.8b00418

APA

Behrendorff, J. B. Y. H., Sandoval-Ibañez, O. A., Sharma, A., & Pribil, M. (2019). Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A. A C S Synthetic Biology, 8(4), 611-620. https://doi.org/10.1021/acssynbio.8b00418

Vancouver

Behrendorff JBYH, Sandoval-Ibañez OA, Sharma A, Pribil M. Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A. A C S Synthetic Biology. 2019 Apr 19;8(4):611-620. https://doi.org/10.1021/acssynbio.8b00418

Author

Behrendorff, James B Y H ; Sandoval-Ibañez, Omar A ; Sharma, Anurag ; Pribil, Mathias. / Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A. In: A C S Synthetic Biology. 2019 ; Vol. 8, No. 4. pp. 611-620.

Bibtex

@article{0f874315bb644ae182d4c94ce68e68e6,
title = "Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A",
abstract = "Protein scaffolding is a useful strategy for controlling the spatial arrangement of cellular components via protein-protein interactions. Protein scaffolding has primarily been used to co-localise soluble proteins in the cytoplasm, but many proteins require membrane association for proper function. Scaffolding at select membrane domains would provide an additional level of control over the distribution of proteins within a cell and could aid in exploiting numerous metabolic pathways that contain membrane-associated enzymes. We developed and characterised a membrane-bound protein scaffolding module based on the thylakoid protein CURT1A. This scaffolding module forms homo-oligomers in the membrane, causing proteins fused to CURT1A to cluster together at membrane surfaces. It is functional in diverse expression hosts and can scaffold proteins at thylakoid membranes in chloroplasts, endoplasmic reticulum in higher plants and Saccharomyces cerevisiae, and the inner membrane of Escherichia coli.",
author = "Behrendorff, {James B Y H} and Sandoval-Iba{\~n}ez, {Omar A} and Anurag Sharma and Mathias Pribil",
year = "2019",
month = apr,
day = "19",
doi = "10.1021/acssynbio.8b00418",
language = "English",
volume = "8",
pages = "611--620",
journal = "ACS Synthetic Biology",
issn = "2161-5063",
publisher = "American Chemical Society",
number = "4",

}

RIS

TY - JOUR

T1 - Membrane-Bound Protein Scaffolding in Diverse Hosts Using Thylakoid Protein CURT1A

AU - Behrendorff, James B Y H

AU - Sandoval-Ibañez, Omar A

AU - Sharma, Anurag

AU - Pribil, Mathias

PY - 2019/4/19

Y1 - 2019/4/19

N2 - Protein scaffolding is a useful strategy for controlling the spatial arrangement of cellular components via protein-protein interactions. Protein scaffolding has primarily been used to co-localise soluble proteins in the cytoplasm, but many proteins require membrane association for proper function. Scaffolding at select membrane domains would provide an additional level of control over the distribution of proteins within a cell and could aid in exploiting numerous metabolic pathways that contain membrane-associated enzymes. We developed and characterised a membrane-bound protein scaffolding module based on the thylakoid protein CURT1A. This scaffolding module forms homo-oligomers in the membrane, causing proteins fused to CURT1A to cluster together at membrane surfaces. It is functional in diverse expression hosts and can scaffold proteins at thylakoid membranes in chloroplasts, endoplasmic reticulum in higher plants and Saccharomyces cerevisiae, and the inner membrane of Escherichia coli.

AB - Protein scaffolding is a useful strategy for controlling the spatial arrangement of cellular components via protein-protein interactions. Protein scaffolding has primarily been used to co-localise soluble proteins in the cytoplasm, but many proteins require membrane association for proper function. Scaffolding at select membrane domains would provide an additional level of control over the distribution of proteins within a cell and could aid in exploiting numerous metabolic pathways that contain membrane-associated enzymes. We developed and characterised a membrane-bound protein scaffolding module based on the thylakoid protein CURT1A. This scaffolding module forms homo-oligomers in the membrane, causing proteins fused to CURT1A to cluster together at membrane surfaces. It is functional in diverse expression hosts and can scaffold proteins at thylakoid membranes in chloroplasts, endoplasmic reticulum in higher plants and Saccharomyces cerevisiae, and the inner membrane of Escherichia coli.

U2 - 10.1021/acssynbio.8b00418

DO - 10.1021/acssynbio.8b00418

M3 - Journal article

C2 - 30884945

VL - 8

SP - 611

EP - 620

JO - ACS Synthetic Biology

JF - ACS Synthetic Biology

SN - 2161-5063

IS - 4

ER -

ID: 215243745