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Reductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorSIRAND-PUGNET, Pascal
hal.structure.identifierInstitut de Biologie Paris Seine [IBPS]
dc.contributor.authorBRÉGEON, Damien
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBÉVEN, Laure
hal.structure.identifierInstitut de Biologie Paris Seine [IBPS]
dc.contributor.authorGOYENVALLE, Catherine
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBLANCHARD, Alain
hal.structure.identifierUniversity of Southern Denmark [SDU]
dc.contributor.authorROSE, Simon
hal.structure.identifierInstitut de Biologie Intégrative de la Cellule [I2BC]
dc.contributor.authorGROSJEAN, Henri
hal.structure.identifierUniversity of Southern Denmark [SDU]
dc.contributor.authorDOUTHWAITE, Stephen
hal.structure.identifierLaboratoire de Chimie des Processus Biologiques [LCPB]
dc.contributor.authorHAMDANE, Djemel
hal.structure.identifierUniversity of Florida [Gainesville] [UF]
dc.contributor.authorCRÉCY-LAGARD, Valérie De
dc.date.issued2020
dc.identifier.issn2218-273X
dc.description.abstractEnThe 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.
dc.description.sponsorshipSorbonne Universités à Paris pour l'Enseignement et la Recherche
dc.language.isoen
dc.publisherMDPI
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subjectMollicutes
dc.subject.enrRNA
dc.subject.enspiroplasmas
dc.subject.entRNA
dc.subject.enmycoplasmas
dc.subject.enmoonlighting function
dc.subject.enacholeplasmas
dc.subject.enbase modification
dc.subject.enevolution
dc.subject.enflavoenzymes
dc.subject.enmethyltransferases
dc.subject.enminimal cell
dc.title.enReductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes
dc.typeArticle de revue
dc.identifier.doi10.3390/biom10040587
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
bordeaux.journalBiomolecules
bordeaux.page587
bordeaux.volume10
bordeaux.issue4
bordeaux.peerReviewedoui
hal.identifierhal-02547879
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02547879v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomolecules&rft.date=2020&rft.volume=10&rft.issue=4&rft.spage=587&rft.epage=587&rft.eissn=2218-273X&rft.issn=2218-273X&rft.au=SIRAND-PUGNET,%20Pascal&BR%C3%89GEON,%20Damien&B%C3%89VEN,%20Laure&GOYENVALLE,%20Catherine&BLANCHARD,%20Alain&rft.genre=article


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