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Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms

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Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms. / Lee, Matthew J.; Mantell, Judith; Hodgson, Lorna; Alibhai, Dominic; Fletcher, Jordan M.; Brown, Ian R.; Frank, Stefanie; Xue, Wei Feng; Verkade, Paul; Woolfson, Derek N.; Warren, Martin J.

In: Nature Chemical Biology, Vol. 14, No. 2, 02.2018, p. 142-147.

Research output: Contribution to journalArticle

Harvard

Lee, MJ, Mantell, J, Hodgson, L, Alibhai, D, Fletcher, JM, Brown, IR, Frank, S, Xue, WF, Verkade, P, Woolfson, DN & Warren, MJ 2018, 'Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms', Nature Chemical Biology, vol. 14, no. 2, pp. 142-147. https://doi.org/10.1038/nchembio.2535

APA

Lee, M. J., Mantell, J., Hodgson, L., Alibhai, D., Fletcher, J. M., Brown, I. R., ... Warren, M. J. (2018). Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms. Nature Chemical Biology, 14(2), 142-147. https://doi.org/10.1038/nchembio.2535

Vancouver

Author

Lee, Matthew J. ; Mantell, Judith ; Hodgson, Lorna ; Alibhai, Dominic ; Fletcher, Jordan M. ; Brown, Ian R. ; Frank, Stefanie ; Xue, Wei Feng ; Verkade, Paul ; Woolfson, Derek N. ; Warren, Martin J. / Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms. In: Nature Chemical Biology. 2018 ; Vol. 14, No. 2. pp. 142-147.

Bibtex

@article{e8d2ced0196e43a1a84e16b0a4e0292b,
title = "Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms",
abstract = "We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two complementary de novo coiled-coil peptides. We show that other proteins can be targeted to this intracellular filamentous arrangement. Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments leading to enhanced ethanol production in these engineered bacterial cells compared with those that do not produce the scaffold. This is consistent with improved metabolic efficiency through enzyme colocation. Finally, the shell-protein scaffold can be directed to the inner membrane of the cell, demonstrating how synthetic cellular organization can be coupled with spatial optimization through in-cell protein design. The cytoscaffold has potential for the development of next-generation cell factories, where it could be used to organize enzyme pathways and metabolite transporters to enhance metabolic flux.",
keywords = "synthetic biology, bacteria, metabolic engineering, protein design",
author = "Lee, {Matthew J.} and Judith Mantell and Lorna Hodgson and Dominic Alibhai and Fletcher, {Jordan M.} and Brown, {Ian R.} and Stefanie Frank and Xue, {Wei Feng} and Paul Verkade and Woolfson, {Derek N.} and Warren, {Martin J.}",
year = "2018",
month = "2",
doi = "10.1038/nchembio.2535",
language = "English",
volume = "14",
pages = "142--147",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "Springer Nature",
number = "2",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - Engineered synthetic scaffolds for organizing proteins within bacterial cytoplasms

AU - Lee, Matthew J.

AU - Mantell, Judith

AU - Hodgson, Lorna

AU - Alibhai, Dominic

AU - Fletcher, Jordan M.

AU - Brown, Ian R.

AU - Frank, Stefanie

AU - Xue, Wei Feng

AU - Verkade, Paul

AU - Woolfson, Derek N.

AU - Warren, Martin J.

PY - 2018/2

Y1 - 2018/2

N2 - We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two complementary de novo coiled-coil peptides. We show that other proteins can be targeted to this intracellular filamentous arrangement. Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments leading to enhanced ethanol production in these engineered bacterial cells compared with those that do not produce the scaffold. This is consistent with improved metabolic efficiency through enzyme colocation. Finally, the shell-protein scaffold can be directed to the inner membrane of the cell, demonstrating how synthetic cellular organization can be coupled with spatial optimization through in-cell protein design. The cytoscaffold has potential for the development of next-generation cell factories, where it could be used to organize enzyme pathways and metabolite transporters to enhance metabolic flux.

AB - We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two complementary de novo coiled-coil peptides. We show that other proteins can be targeted to this intracellular filamentous arrangement. Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments leading to enhanced ethanol production in these engineered bacterial cells compared with those that do not produce the scaffold. This is consistent with improved metabolic efficiency through enzyme colocation. Finally, the shell-protein scaffold can be directed to the inner membrane of the cell, demonstrating how synthetic cellular organization can be coupled with spatial optimization through in-cell protein design. The cytoscaffold has potential for the development of next-generation cell factories, where it could be used to organize enzyme pathways and metabolite transporters to enhance metabolic flux.

KW - synthetic biology

KW - bacteria

KW - metabolic engineering

KW - protein design

UR - http://www.scopus.com/inward/record.url?scp=85040862509&partnerID=8YFLogxK

U2 - 10.1038/nchembio.2535

DO - 10.1038/nchembio.2535

M3 - Article

C2 - 29227472

AN - SCOPUS:85040862509

VL - 14

SP - 142

EP - 147

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 2

ER -