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@article{2330800,
author = {Sandor, Andras and Šámalová, Markéta and Brandizzi, Federica and Kriechbaumer, Verena and Moore, Ian and Fricker, Mark D. and Sweetlove, Fricker},
article_number = {1},
doi = {http://dx.doi.org/10.1093/jxb/erad364},
keywords = {Compartment; endoplasmic reticulum; membrane; OSER; proliferation; synthetic biology},
language = {eng},
issn = {0022-0957},
journal = {Journal of Experimental Botany},
title = {Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins},
url = {https://doi.org/10.1093/jxb/erad364},
volume = {75},
year = {2024}
}
TY - JOUR
ID - 2330800
AU - Sandor, Andras - Šámalová, Markéta - Brandizzi, Federica - Kriechbaumer, Verena - Moore, Ian - Fricker, Mark D. - Sweetlove, Fricker
PY - 2024
TI - Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins
JF - Journal of Experimental Botany
VL - 75
IS - 1
SP - 45-59
EP - 45-59
PB - Oxford University Press
SN - 00220957
KW - Compartment
KW - endoplasmic reticulum
KW - membrane
KW - OSER
KW - proliferation
KW - synthetic biology
UR - https://doi.org/10.1093/jxb/erad364
N2 - The endoplasmic reticulum (ER) is a dynamic organelle that is amenable to major restructuring. Introduction of recombinant ER-membrane-resident proteins that form homo oligomers is a known method of inducing ER proliferation: interaction of the proteins with each other alters the local structure of the ER network, leading to the formation large aggregations of expanded ER, sometimes leading to the formation of organized smooth endoplasmic reticulum (OSER). However, these membrane structures formed by ER proliferation are poorly characterized and this hampers their potential development for plant synthetic biology. Here, we characterize a range of ER-derived membranous compartments in tobacco and show how the nature of the polyproteins introduced into the ER membrane affect the morphology of the final compartment. We show that a cytosol-facing oligomerization domain is an essential component for compartment formation. Using fluorescence recovery after photobleaching, we demonstrate that although the compartment retains a connection to the ER, a diffusional barrier exists to both the ER and the cytosol associated with the compartment. Using quantitative image analysis, we also show that the presence of the compartment does not disrupt the rest of the ER network. Moreover, we demonstrate that it is possible to recruit a heterologous, bacterial enzyme to the compartment, and for the enzyme to accumulate to high levels. Finally, transgenic Arabidopsis constitutively expressing the compartment-forming polyproteins grew and developed normally under standard conditions.
ER -
SANDOR, Andras, Markéta ŠÁMALOVÁ, Federica BRANDIZZI, Verena KRIECHBAUMER, Ian MOORE, Mark D. FRICKER and Fricker SWEETLOVE. Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins. \textit{Journal of Experimental Botany}. Oxford University Press, 2024, vol.~75, No~1, p.~45-59. ISSN~0022-0957. Available from: https://dx.doi.org/10.1093/jxb/erad364.
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