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Nova · Professor Researcher · re-ranking top 20…

Betül Kaçar

· a professor of bacteriology

University of Wisconsin-Madison · Bacteriology

Active 2012–2024

h-index23
Citations1.6k
Papers11168 last 5y
Funding$353k
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Research topics

  • Biology
  • Evolutionary biology
  • Biochemistry
  • Astrobiology
  • Engineering ethics
  • Aeronautics
  • Computational biology
  • Genetics
  • Inorganic chemistry
  • Paleontology
  • Chemistry
  • Engineering
  • Aerospace engineering

Selected publications

  • On the Past, Present, and Future Role of Biology in NASA’s Exploration of our Solar System

    Bulletin of the AAS · 2021 · 1 citations

    • Astrobiology
    • Engineering ethics
    • Aeronautics

    Here we provide a brief perspective on the role of biology in NASA’s planetary science goals, and its spacecraft missions, past, present, and future. We argue that while biology - via astrobiology - generates much interest and excitement for NASA, biology is vastly under-represented as a science within NASA Planetary Science Division missions.

  • Cofactors are Remnants of Life’s Origin and Early Evolution

    Journal of Molecular Evolution · 2021 · 105 citations

    Senior authorCorresponding
    • Biology
    • Genetics
    • Biochemistry

    The RNA World is one of the most widely accepted hypotheses explaining the origin of the genetic system used by all organisms today. It proposes that the tripartite system of DNA, RNA, and proteins was preceded by one consisting solely of RNA, which both stored genetic information and performed the molecular functions encoded by that genetic information. Current research into a potential RNA World revolves around the catalytic properties of RNA-based enzymes, or ribozymes. Well before the discovery of ribozymes, Harold White proposed that evidence for a precursor RNA world could be found within modern proteins in the form of coenzymes, the majority of which contain nucleobases or nucleoside moieties, such as Coenzyme A and S-adenosyl methionine, or are themselves nucleotides, such as ATP and NADH (a dinucleotide). These coenzymes, White suggested, had been the catalytic active sites of ancient ribozymes, which transitioned to their current forms after the surrounding ribozyme scaffolds had been replaced by protein apoenzymes during the evolution of translation. Since its proposal four decades ago, this groundbreaking hypothesis has garnered support from several different research disciplines and motivated similar hypotheses about other classes of cofactors, most notably iron-sulfur cluster cofactors as remnants of the geochemical setting of the origin of life. Evidence from prebiotic geochemistry, ribozyme biochemistry, and evolutionary biology, increasingly supports these hypotheses. Certain coenzymes and cofactors may bridge modern biology with the past and can thus provide insights into the elusive and poorly-recorded period of the origin and early evolution of life.

  • Reconstructing the evolutionary history of nitrogenases: Evidence for ancestral molybdenum‐cofactor utilization

    Geobiology · 2020 · 122 citations

    Senior authorCorresponding
    • Evolutionary biology
    • Biology
    • Chemistry

    The nitrogenase metalloenzyme family, essential for supplying fixed nitrogen to the biosphere, is one of life's key biogeochemical innovations. The three forms of nitrogenase differ in their metal dependence, each binding either a FeMo-, FeV-, or FeFe-cofactor where the reduction of dinitrogen takes place. The history of nitrogenase metal dependence has been of particular interest due to the possible implication that ancient marine metal availabilities have significantly constrained nitrogenase evolution over geologic time. Here, we reconstructed the evolutionary history of nitrogenases, and combined phylogenetic reconstruction, ancestral sequence inference, and structural homology modeling to evaluate the potential metal dependence of ancient nitrogenases. We find that active-site sequence features can reliably distinguish extant Mo-nitrogenases from V- and Fe-nitrogenases and that inferred ancestral sequences at the deepest nodes of the phylogeny suggest these ancient proteins most resemble modern Mo-nitrogenases. Taxa representing early-branching nitrogenase lineages lack one or more biosynthetic nifE and nifN genes that both contribute to the assembly of the FeMo-cofactor in studied organisms, suggesting that early Mo-nitrogenases may have utilized an alternate and/or simplified pathway for cofactor biosynthesis. Our results underscore the profound impacts that protein-level innovations likely had on shaping global biogeochemical cycles throughout the Precambrian, in contrast to organism-level innovations that characterize the Phanerozoic Eon.

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