{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Huang L"],"funding":["National Natural Science Foundation of China","Agriculture Research System of China"],"pubmed_abstract":["<i>Riemerella anatipestifer</i> ATCC11845 (RA ATCC11845) is naturally competent. However, the genes involved in natural transformation in this species remain largely unknown. Bioinformatic analysis predicts that DprA of RA (DprA<sub>Ra</sub>) has three domains: a sterile alpha motif (SAM), a Rossmann fold (RF) domain and a Z-DNA-binding domain (Zα). Inactivation of <i>dprA</i> abrogated natural transformation in RA ATCC11845, and this effect was restored by the expression of <i>dprA in trans</i>. The <i>dprA</i> with SAM and RF domains of <i>Streptococcus pneumoniae</i> and the <i>dprA</i> with RF and Zα domains of <i>Helicobacter pylori</i> was able to restore natural transformation in the RA ATCC11845 <i>dprA</i> mutant. An Arg123 mutation in the RF domain of <i>R. anatipestifer</i> was not able to restore natural transformation of the RA ATCC11845 <i>dprA</i> mutant. Furthermore, DprA<sup>R123E</sup> abolished its ability to bind DNA, suggesting that the RF domain is essential for the function of DprA. Finally, the <i>dprA</i> of <i>Fusobacterium naviforme</i> which has not been reported to be natural competent currently was partially able to restore natural transformation in RA ATCC11845 <i>dprA</i> mutant. These results collectively suggest that DprA has a conserved evolutionary mechanism."],"journal":["Frontiers in genetics"],"pagination":["429"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6533540"],"repository":["biostudies-literature"],"pubmed_title":["DprA Is Essential for Natural Competence in <i>Riemerella anatipestifer</i> and Has a Conserved Evolutionary Mechanism."],"pmcid":["PMC6533540"],"pubmed_authors":["Biville F","Liu M","Huang J","Cheng A","Tian B","Huang L","Zhang L","Zhang S","Zhu D","Zhao X","Wang M","Rehman MU","Liu Y","Tian X","Jia R","Yang Q","Chen X","Chen S","Pan L","Wu Y","Yu Y"],"additional_accession":[]},"is_claimable":false,"name":"DprA Is Essential for Natural Competence in <i>Riemerella anatipestifer</i> and Has a Conserved Evolutionary Mechanism.","description":"<i>Riemerella anatipestifer</i> ATCC11845 (RA ATCC11845) is naturally competent. However, the genes involved in natural transformation in this species remain largely unknown. Bioinformatic analysis predicts that DprA of RA (DprA<sub>Ra</sub>) has three domains: a sterile alpha motif (SAM), a Rossmann fold (RF) domain and a Z-DNA-binding domain (Zα). Inactivation of <i>dprA</i> abrogated natural transformation in RA ATCC11845, and this effect was restored by the expression of <i>dprA in trans</i>. The <i>dprA</i> with SAM and RF domains of <i>Streptococcus pneumoniae</i> and the <i>dprA</i> with RF and Zα domains of <i>Helicobacter pylori</i> was able to restore natural transformation in the RA ATCC11845 <i>dprA</i> mutant. An Arg123 mutation in the RF domain of <i>R. anatipestifer</i> was not able to restore natural transformation of the RA ATCC11845 <i>dprA</i> mutant. Furthermore, DprA<sup>R123E</sup> abolished its ability to bind DNA, suggesting that the RF domain is essential for the function of DprA. Finally, the <i>dprA</i> of <i>Fusobacterium naviforme</i> which has not been reported to be natural competent currently was partially able to restore natural transformation in RA ATCC11845 <i>dprA</i> mutant. These results collectively suggest that DprA has a conserved evolutionary mechanism.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2025-05-18T13:15:08.694Z","creation":"2025-05-18T13:15:08.694Z"},"accession":"S-EPMC6533540","cross_references":{"pubmed":["31156696"],"doi":["10.3389/fgene.2019.00429"]}}