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

James B Y H Behrendorff; Omar A Sandoval-Ibañez; Anurag Sharma; Mathias Pribil

doi:10.1021/acssynbio.8b00418

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

James B Y H Behrendorff, Omar A Sandoval-Ibañez, Anurag Sharma, Mathias Pribil

Molekylær Plantebiologi

4 Citationer (Scopus)

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 colocalize 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 characterized 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.

Originalsprog	Engelsk
Tidsskrift	A C S Synthetic Biology
Vol/bind	8
Udgave nummer	4
Sider (fra-til)	611-620
ISSN	2161-5063
DOI	https://doi.org/10.1021/acssynbio.8b00418
Status	Udgivet - 19 apr. 2019

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10.1021/acssynbio.8b00418

Citationsformater

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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 colocalize 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 characterized 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",

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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 colocalize 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 characterized 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 colocalize 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 characterized 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

SN - 2161-5063

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JO - ACS Synthetic Biology

JF - ACS Synthetic Biology

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ER -

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

Abstract

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