Evolution of the Ubiquitin-Activating Enzyme Uba1 (E1)
Douglas C. Allan, J. C. Phillips
TL;DR
This paper investigates the evolutionary development of the ubiquitin-activating enzyme Uba1 (E1) across different species, linking its size and sequence changes to thermodynamic principles.
Contribution
It introduces a thermodynamic scaling approach to understand Uba1 evolution from simple to complex organisms.
Findings
Uba1 evolved modestly from slime mold to humans.
Uba1 is over 14 times larger than ubiquitin.
Evolution correlates with subtle amino acid sequence changes.
Abstract
Ubiquitin tags diseased proteins and initiates an enzyme conjugation cascade, which has three stages. The first-stage enzyme Uba1 (E1) has evolved only modestly from slime mold to humans, and is > 14 times larger than Ub. Here we use critical point thermodynamic scaling theory to connect Uba1 (E1) evolution from yeast and slime mold to fruit flies and humans to subtle changes in its amino acid sequences.
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