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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Prions: Beyond a Single Protein.

Alvin S Das1, Wen-Quan Zou2

  • 1Departments of Pathology and Neurology, National Prion Disease Pathology Surveillance Center, National Center for Regenerative Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.

Clinical Microbiology Reviews
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Summary
This summary is machine-generated.

Prions, infectious proteins, are derived from normal cellular proteins and lack genetic material. Prion-like behavior is now recognized in various cellular proteins, extending beyond disease to physiological roles.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Infectious Diseases

Background:

  • Cellular proteins were historically considered exclusively beneficial.
  • Griffith's 1967 hypothesis proposed proteins as infectious pathogens.
  • Prions were identified as infectious particles composed of protein in 1982.

Purpose of the Study:

  • To review the discovery and unique nature of prions.
  • To explore the concept of prion-like behavior in other cellular proteins.
  • To discuss the broader implications of prion biology.

Main Methods:

  • Historical review of prion research.
  • Analysis of prion structure and replication.
  • Examination of recent findings on prion-like proteins.

Main Results:

  • Prions are infectious pathogens originating from endogenous cellular forms.
  • Prions lack DNA or RNA, with information encoded in protein conformation.
  • Prion-like behavior is observed in proteins with both pathogenic and physiological functions.

Conclusions:

  • Prion biology extends beyond transmissible spongiform encephalopathies.
  • Understanding prion-like mechanisms is crucial for diverse biological processes.
  • The field of prion biology has significant implications for medicine and cell biology.