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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Archaeal viruses play a crucial role in the ecosystems of extremophilic archaea, particularly those belonging to the phyla Euryarchaeota and Crenarchaeota. By shaping host evolution and facilitating gene transfer, these viruses influence microbial communities and contribute to genetic diversity in extreme environments. The archaea they infect thrive in acidic hot springs and hydrothermal vents characterized by high temperatures and low pH. Archaeal viruses exhibit remarkable structural...
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The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
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Experimental Approaches for Biochemical Analysis of Glial Fibrillary Acidic Protein and Its Disease-associated Variants
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Fibrillarin from Archaea to human.

Ulises Rodriguez-Corona1, Margarita Sobol2, Luis Carlos Rodriguez-Zapata3

  • 1Unidad de Bioquímica y Biología molecular de plantas, Centro de Investigación Científica de Yucatán, Colonia Chuburná de Hidalgo, Mérida, Yucatan, Mexico.

Biology of the Cell
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Fibrillarin, a key protein in ribosome biogenesis and a cancer marker, is explored for its structure, interactions, and role in viral infections. Its expression is linked to cancer, especially when the p53 tumor suppressor is low.

Keywords:
CancerMethylationRNA processingRibosomal biogenesisp53

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Fibrillarin is an essential protein and a marker for RNA polymerase I transcription.
  • Its methyltransferase activity is crucial for preribosomal RNA processing and ribosome stability.
  • Elevated fibrillarin levels correlate with cancer, particularly when p53, a negative regulator, is diminished.

Purpose of the Study:

  • To investigate the conserved domains, structure, and interacting molecules of fibrillarin.
  • To explore fibrillarin's involvement in various cellular processes.
  • To examine fibrillarin interactions with viral proteins during infection.

Main Methods:

  • Bioinformatic analysis of fibrillarin domain conservation.
  • Structural analysis of fibrillarin.
  • Identification of interacting molecules through biochemical assays.
  • Analysis of fibrillarin interactions during viral infections.

Main Results:

  • Demonstrated conserved domains and structural features of fibrillarin across species.
  • Identified diverse cellular molecules interacting with fibrillarin.
  • Revealed interactions between fibrillarin and viral proteins during infection.

Conclusions:

  • Fibrillarin plays a conserved role in cellular processes and ribosome biogenesis.
  • Fibrillarin interacts with a range of cellular and viral factors.
  • Further research into fibrillarin's function may offer insights into cancer and viral pathogenesis.