SIRAND-PUGNET, Pascal; BRÉGEON, Damien; BÉVEN, Laure; GOYENVALLE, Catherine; BLANCHARD, Alain; ROSE, Simon; GROSJEAN, Henri; DOUTHWAITE, Stephen; HAMDANE, Djemel; CRÉCY-LAGARD, Valérie De

doi:10.3390/biom10040587

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SIRAND-PUGNET, Pascal
Biologie du fruit et pathologie [BFP]

BRÉGEON, Damien
Institut de Biologie Paris Seine [IBPS]

BÉVEN, Laure
Biologie du fruit et pathologie [BFP]

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Article de revue

Ce document a été publié dans

Biomolecules. 2020, vol. 10, n° 4, p. 587

MDPI

Résumé en anglais

The C5-methylation of uracil to form 5-methyluracil (m5U) is a ubiquitous base modification of nucleic acids. Four enzyme families have converged to catalyze this methylation using different chemical solutions. Here, we investigate the evolution of 5-methyluracil synthase families in Mollicutes, a class of bacteria that has undergone extensive genome erosion. Many mollicutes have lost some of the m5U methyltransferases present in their common ancestor. Cases of duplication and subsequent shift of function are also described. For example, most members of the Spiroplasma subgroup use the ancestral tetrahydrofolate-dependent TrmFO enzyme to catalyze the formation of m5U54 in tRNA, while a TrmFO paralog (termed RlmFO) is responsible for m5U1939 formation in 23S rRNA. RlmFO has replaced the S-adenosyl-L-methionine (SAM)-enzyme RlmD that adds the same modification in the ancestor and which is still present in mollicutes from the Hominis subgroup. Another paralog of this family, the TrmFO-like protein, has a yet unidentified function that differs from the TrmFO and RlmFO homologs. Despite having evolved towards minimal genomes, the mollicutes possess a repertoire of m5U-modifying enzymes that is highly dynamic and has undergone horizontal transfer.< Réduire

Mots clés

Mollicutes

Mots clés en anglais

rRNA

spiroplasmas

tRNA

mycoplasmas

moonlighting function

acholeplasmas

base modification

evolution

flavoenzymes

methyltransferases

minimal cell

DOI

http://dx.doi.org/10.3390/biom10040587

Project ANR

Sorbonne Universités à Paris pour l'Enseignement et la Recherche - ANR-11-IDEX-0004

Origine

Importé de hal

Unités de recherche

Biologie du Fruit & Pathologie (BFP) - UMR 1332