5 research outputs found

    George Walters-Marrah, \u2720

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    I am a junior at UCF majoring in biotechnology and biomedical sciences with an emphasis on molecular microbiology. I find microbial pathogens and how they interact with the environment extraordinarily interesting. I currently study mycobacteria in Dr.Kyle Rohde\u27s research lab at the UCF Burnett School of Biomedical Sciences. My career aspirations are to obtain a Ph.D. relating to immunity and pathogenesis, go into either academia or the biotechnology industry, and possibly start a biotech business based on a conceptual computer program that I am brainstorming about.https://stars.library.ucf.edu/mcnair_gallery/1107/thumbnail.jp

    Structural characterization of NrnC identifies unifying features of diribonucleotidases

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    RNA degradation is fundamental for cellular homeostasis. The process is carried out by various classes of endolytic and exolytic enzymes that together degrade an RNA polymer to mono-ribonucleotides. Within the exoribonucleases, nano-RNases play a unique role as they act on the smallest breakdown products and hence catalyze the final steps in the process. We recently showed that oligoribonuclease (Orn) acts as a dedicated diribonucleotidase, defining the ultimate step in RNA degradation that is crucial for cellular fitness (Kim et al., 2019). Whether such a specific activity exists in organisms that lack Orn-type exoribonucleases remained unclear. Through quantitative structure-function analyses we show here that NrnC-type RNases share this narrow substrate preference with Orn. Although NrnC employs similar structural features that distinguish these two classes as diribonucleotidases from other exoribonucleases, these key determinants for diribonucleotidase activity are realized through distinct structural scaffolds. The structures together with comparative genomic analyses of the phylogeny of DEDD-type exoribonucleases indicates convergent evolution as the mechanism of how diribonucleotidase activity emerged repeatedly in various organisms. The evolutionary pressure to maintain diribonucleotidase activity further underlines the important role these analogous proteins play for cell growth

    Correction: Structural characterization of NrnC identifies unifying features of dinucleases

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    After publication, we realized that the designations ‘nucleotidase’ (used as ‘diribonucleotidase’ or ‘dinucleotidase’ in the manuscript) have been reserved for a different enzymatic reaction than the one described in the manuscript. The term ‘nucleotidase’ usually refers to enzymes that hydrolyze nucleotides into nucleosides and phosphate. However, the enzymes under investigation in this study cleave a phosphodiester bond, converting dinucleotides into mononucleotides, which would be appropriately described as ‘nuclease’ activity, or more precisely, ‘diribonuclease’ or ‘dinuclease’ activity. This change in terminology has no impact on any of the results, their interpretation, or discussions reported in the paper; on the contrary, the correction will prevent any potential confusion regarding the chemical reaction we report on.We have corrected the manuscript to refer to the appropriate enzyme classification by replacing all instances of ‘diribonucleotidase’ and ‘dinucleotidase’ with ‘diribonuclease’ and ‘dinuclease’, respectively
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