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

Investigación publicada en eLife

15 de diciembre de 2020

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




Escudero JA., Nivina A., Kemble HE., Loot C., Tenaillon O. y Mazel D.




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

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



Participantes:

Institut PasteurBacterial Genome Plasticity (BGP). Department of Genomes and Genetics. Institut Pasteur.

Centre National de la Recherche ScientifiqueCentre National de la Recherche Scientifique (CNRS).

Universidad ComplutenseDepartamento de Sanidad Animal. Facultad de Veterinaria. Universidad Complutense (UCM).

Universidad ComplutenseServicio de Zoonosis de Transmisión Alimentaria y Resistencia a Antimicrobianos (ZTA). Centro de Vigilancia Sanitaria Veterinaria (VISAVET). Universidad Complutense (UCM).

Université Sorbonne Paris DescartesUniversité Sorbonne Paris Descartes.

Université Paris DiderotUniversité Paris Diderot.

Institut national de la santé et de la recherche médicaleInstitut national de la santé et de la recherche médicale (INSERM).







eLife
FACTOR YEAR Q
8.140 2020

PMID: 33319743

ISSN: 2050-084X



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


REVISTA: eLife


NUMERACIÓN: 9:e58061


AÑO: 2020


EDITORIAL: ELIFE SCIENCES PUBLICATIONS LTD


AUTORES: Escudero JA., Nivina A., Kemble HE., Loot C., Tenaillon O. and Mazel D.


José Antonio Escudero García-Calderón

DOI: https://doi.org/10.7554/elife.58061


CITA ESTA PUBLICACIÓN:

Escudero JA., Nivina A., Kemble HE., Loot C., Tenaillon O. y Mazel D. Primary and promiscuous functions coexist during evolutionary innovation through whole protein domain acquisitions. eLife. 9:e58061. 2020. (A). ISSN: 2050-084X. DOI: 10.7554/elife.58061


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