Primary and promiscuous functions coexist during evolutionary innovation through whole protein domain acquisitions

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Escudero García-Calderón, José Antonio and Nivina, Aleksandra and Kemble, Harry E and Loot, Céline and Tenaillon, Olivier and Mazel, Didier (2020) Primary and promiscuous functions coexist during evolutionary innovation through whole protein domain acquisitions. eLife, 9 . ISSN 2050-084X

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Official URL: https://doi.org/10.7554/eLife.58061



Abstract

Molecular examples of evolutionary innovation are scarce and generally involve point mutations. Innovation can occur through larger rearrangements, but here experimental data is extremely limited. Integron integrases innovated from double-strand- toward single-strand-DNA recombination through the acquisition of the I2 a-helix. To investigate how this transition was possible, we have evolved integrase IntI1 to what should correspond to an early innovation state by selecting for its ancestral activity. Using synonymous alleles to enlarge sequence space exploration, we have retrieved 13 mutations affecting both I2 and the multimerization domains of IntI1. We circumvented epistasis constraints among them using a combinatorial library that revealed their individual and collective fitness effects. We obtained up to 104 -fold increases in ancestral activity with various asymmetrical trade-offs in single-strand-DNA recombination. We show that high levels of primary and promiscuous functions could have initially coexisted following I2 acquisition, paving the way for a gradual evolution toward innovation.


Item Type:Article
Subjects:Medical sciences > Medicine > Medical microbiology
Medical sciences > Veterinary > Microbiology
Medical sciences > Biology > Evolution
Medical sciences > Biology > Genetics
Medical sciences > Biology > Microbiology
ID Code:70811
Deposited On:28 Feb 2022 11:06
Last Modified:28 Feb 2022 11:14

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