biostudies-literatureUnknown10Huang LNational Natural Science Foundation of ChinaAgriculture Research System of China<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_Ra) 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^R123E 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.Frontiers in genetics429https://www.ebi.ac.uk/biostudies/studies/S-EPMC6533540biostudies-literatureDprA Is Essential for Natural Competence in <i>Riemerella anatipestifer</i> and Has a Conserved Evolutionary Mechanism.PMC6533540Biville FLiu MHuang JCheng ATian BHuang LZhang LZhang SZhu DZhao XWang MRehman MULiu YTian XJia RYang QChen XChen SPan LWu YYu YfalseDprA Is Essential for Natural Competence in <i>Riemerella anatipestifer</i> and Has a Conserved Evolutionary Mechanism.<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_Ra) 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^R123E 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.2019-01-01T00:00:00Z20192025-05-18T13:15:08.694Z2025-05-18T13:15:08.694ZS-EPMC65335403115669610.3389/fgene.2019.00429