J 2024

Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins

SANDOR, Andras, Markéta ŠÁMALOVÁ, Federica BRANDIZZI, Verena KRIECHBAUMER, Ian MOORE et. al.

Basic information

Original name

Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins

Authors

SANDOR, Andras, Markéta ŠÁMALOVÁ (203 Czech Republic, belonging to the institution), Federica BRANDIZZI, Verena KRIECHBAUMER, Ian MOORE, Mark D. FRICKER and Fricker SWEETLOVE (guarantor)

Edition

Journal of Experimental Botany, Oxford University Press, 2024, 0022-0957

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10611 Plant sciences, botany

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 6.900 in 2022

Organization unit

Faculty of Science

DOI

UT WoS

001086238800001

Keywords in English

Compartment; endoplasmic reticulum; membrane; OSER; proliferation; synthetic biology

Tags

Tags

International impact, Reviewed
Změněno: 18/1/2024 10:15, Mgr. Marie Šípková, DiS.

Abstract

V originále

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.