Ancestral protein reconstruction uncovers unanticipated properties of the ancestral Arf protein and of modern Arf1
Abstract
The period of eukaryogenesis between the merger of prokaryotic lineages and the last eukaryotic common ancestor (LECA) involved an increase in cellular complexity, including appearance of internal organelles. Membrane trafficking linking organelles is regulated by Arf family GTPases, including Arf1 and Arf6, both present in LECA. Here we use ancestral sequence reconstruction and molecular cell biological characterization to explore the properties of the ancestor of the Arf1 and Arf6 GTPases. The predicted ancestral Arf1/6 proteins localize to both the Golgi, like Arf1, and the plasma membrane, like Arf6. We find that localization to the plasma membrane is due to a C-terminal polybasic motif that unexpectedly is also found in modern Arf1 proteins from a wide diversity of eukaryotes. Our data suggest that the ancestral Arf1/6 protein was a generalist, acting at internal compartments and the cell periphery, a feature preserved in diverse extant Arf1 proteins.
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BibTeX
@misc{alves2026ancestral,
title = {{Ancestral protein reconstruction uncovers unanticipated properties of the ancestral Arf protein and of modern Arf1}},
author = {Marine Alves and Mandeep Sivia and Kristína Záhonová and Catherine L Jackson and Joel B Dacks},
howpublished = {HAL},
year = {2026},
month = oct,
url = {https://hal.science/hal-05843667v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - UNPB
TI - Ancestral protein reconstruction uncovers unanticipated properties of the ancestral Arf protein and of modern Arf1
AU - Marine Alves
AU - Mandeep Sivia
AU - Kristína Záhonová
AU - Catherine L Jackson
AU - Joel B Dacks
PY - 2026
DA - 2026/10/29
PB - HAL
UR - https://hal.science/hal-05843667v1
AB - The period of eukaryogenesis between the merger of prokaryotic lineages and the last eukaryotic common ancestor (LECA) involved an increase in cellular complexity, including appearance of internal organelles. Membrane trafficking linking organelles is regulated by Arf family GTPases, including Arf1 and Arf6, both present in LECA. Here we use ancestral sequence reconstruction and molecular cell biological characterization to explore the properties of the ancestor of the Arf1 and Arf6 GTPases. The predicted ancestral Arf1/6 proteins localize to both the Golgi, like Arf1, and the plasma membrane, like Arf6. We find that localization to the plasma membrane is due to a C-terminal polybasic motif that unexpectedly is also found in modern Arf1 proteins from a wide diversity of eukaryotes. Our data suggest that the ancestral Arf1/6 protein was a generalist, acting at internal compartments and the cell periphery, a feature preserved in diverse extant Arf1 proteins.
ER -