Fungal prion

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(Redirected from PSI (prion))

Fungal prions are unique proteins found in fungi that exhibit prion-like characteristics. These proteins can misfold in a similar manner to prion proteins in animals, leading to heritable changes in phenotype without alterations in the underlying DNA. The study of fungal prions has significantly contributed to our understanding of prion biology, including the mechanisms of protein misfolding and aggregation, and their effects on cellular functions.

Characteristics[edit | edit source]

Fungal prions differ from their animal counterparts in that they are generally not associated with disease. Instead, they can affect traits such as metabolism, morphology, and development in fungi. The most well-known fungal prion is the Sup35 protein in Saccharomyces cerevisiae (baker's yeast), which, when in its prion form, can alter the fidelity of translation, leading to a variety of phenotypic outcomes.

Mechanism[edit | edit source]

The prion form of a fungal protein is typically a beta-sheet-rich, amyloid-like structure that can induce the normally folded version of the protein to adopt the prion conformation. This self-propagating misfolding mechanism is key to the prion phenomenon. In fungi, the presence of prions can be beneficial, neutral, or detrimental to the host, depending on the environmental context and the specific functions of the prion-forming protein.

Detection and Study[edit | edit source]

Fungal prions are detected using a variety of biochemical and genetic techniques, including protein aggregation assays, fluorescence microscopy, and genetic screens for prion loss or gain of function. The study of these prions has provided insights into the cellular mechanisms of protein folding, aggregation, and the regulation of protein function.

Implications[edit | edit source]

The existence of fungal prions challenges the traditional view of genetics by demonstrating that heritable information can be transmitted through changes in protein conformation rather than changes in DNA sequence. This has implications for understanding diseases caused by prion proteins in humans and animals, as well as for the broader fields of genetics and molecular biology.

Examples[edit | edit source]

Besides Sup35, other examples of fungal prions include Ure2 in Saccharomyces cerevisiae, which affects nitrogen metabolism, and HET-s in Podospora anserina, involved in a fungal self/non-self recognition system.

Research and Applications[edit | edit source]

Research on fungal prions continues to uncover the diverse roles these proteins play in fungal biology and evolution. Understanding how prions affect fungal traits can lead to applications in biotechnology, such as the development of new strategies for controlling fungal pathogens or for harnessing fungi for industrial purposes.


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Contributors: Prab R. Tumpati, MD