Function of Ribonucleotide Reductase-Encoding Genes in Flavobacterium johnsoniae
Start Date
15-4-2021 2:00 PM
End Date
15-4-2021 3:00 PM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
Yongtao Zhu
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
Ribonucleotide reductases (RNRs) are essential enzymes for all living organisms. These enzymes convert ribonucleotides to 2’-deoxyribonucleotides, molecules that are required for the synthesis of DNA. Bacterial RNRs have a variety of activation mechanisms that, in many pathogenic bacteria, differ from those used in human cells. This makes them an ideal target for antibiotic treatments. RNRs are divided into three distinct classes: Classes I, II, and III. Class I RNRs are divided into five subclasses (a-e). Many organisms have more than one class of RNR and new RNRs are still being discovered. Class Id, a novel RNR subclass, was shown to have an activation mechanism unlike previously studied class I RNRs. This enzyme has been shown in vitro to scavenge manganese and superoxide from the environment to become activated. To create an effective RNR targeting antibiotic, it needs to be understood how these enzymes function in vivo. The goal of this research is to investigate how RNRs function inside a bacterial cell. Flavobacterium johnsoniae was selected as the model organism for this study as it is the bacteria in which the class Id RNR was discovered, and in this organism targeted genes can be easily manipulated. Analysis of F. johnsoniae shows that it has genes for two Class I RNR enzymes: Ia and Id. We have generated 15 mutants lacking genes encoding the class I RNRs, manganese transporter, and two superoxide dismutases. The growth of these 15 strains is currently being analyzed under varying growth conditions in order to understand how they function. The growth results will reveal if endogenous changes of the manganese or superoxide levels can affect the activation of the Id RNR in vivo. This research could provide the basis for the development of future antibiotic drugs that target these essential enzymes in pathogenic bacteria.
Function of Ribonucleotide Reductase-Encoding Genes in Flavobacterium johnsoniae
Ribonucleotide reductases (RNRs) are essential enzymes for all living organisms. These enzymes convert ribonucleotides to 2’-deoxyribonucleotides, molecules that are required for the synthesis of DNA. Bacterial RNRs have a variety of activation mechanisms that, in many pathogenic bacteria, differ from those used in human cells. This makes them an ideal target for antibiotic treatments. RNRs are divided into three distinct classes: Classes I, II, and III. Class I RNRs are divided into five subclasses (a-e). Many organisms have more than one class of RNR and new RNRs are still being discovered. Class Id, a novel RNR subclass, was shown to have an activation mechanism unlike previously studied class I RNRs. This enzyme has been shown in vitro to scavenge manganese and superoxide from the environment to become activated. To create an effective RNR targeting antibiotic, it needs to be understood how these enzymes function in vivo. The goal of this research is to investigate how RNRs function inside a bacterial cell. Flavobacterium johnsoniae was selected as the model organism for this study as it is the bacteria in which the class Id RNR was discovered, and in this organism targeted genes can be easily manipulated. Analysis of F. johnsoniae shows that it has genes for two Class I RNR enzymes: Ia and Id. We have generated 15 mutants lacking genes encoding the class I RNRs, manganese transporter, and two superoxide dismutases. The growth of these 15 strains is currently being analyzed under varying growth conditions in order to understand how they function. The growth results will reveal if endogenous changes of the manganese or superoxide levels can affect the activation of the Id RNR in vivo. This research could provide the basis for the development of future antibiotic drugs that target these essential enzymes in pathogenic bacteria.
