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Is there a human [psi]?

O Jean-Jean1, X Le Goff, M Philippe

  • 1Laboratoire de génétique moléculaire, URA 1302 CNRS, Ecole normale supérieure, Paris, France.

Comptes Rendus De L'Academie Des Sciences. Serie III, Sciences De La Vie
|June 1, 1996
PubMed
Summary
This summary is machine-generated.

The human SUP35 gene encodes a longer Sup35p protein than previously known, with prion-like properties similar to yeast. This longer form is prevalent in human and mouse tissues, suggesting conserved functions in translation termination.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Prion Biology

Background:

  • The yeast Sup35p protein is crucial for translation termination and the [psi] phenotype.
  • Prion-like properties of the [psi] determinant were previously localized to the N-terminal 114 amino acids of yeast Sup35p.
  • The full-length human SUP35 gene and its protein product's characteristics were not fully elucidated.

Purpose of the Study:

  • To investigate the complete open reading frame of the human SUP35 gene.
  • To determine the translation initiation site and the major form of human Sup35p.
  • To explore potential prion-like properties of human Sup35p and its presence in mammalian tissues.

Main Methods:

  • Sequence analysis to identify the full 5' end of the human SUP35 gene.
  • Cell transfection experiments in human cells to study protein expression.
  • Western blotting to detect and characterize Sup35p protein forms in human and mouse tissues.

Main Results:

  • The human SUP35 gene's open reading frame is 138 codons longer than previously reported.
  • Translation initiates at the first AUG, producing a longer human Sup35p protein form.
  • This extended Sup35p protein is the major form in human cells and has an analog in mouse tissues.

Conclusions:

  • The human SUP35 gene encodes a significantly longer Sup35p protein, including an N-terminal extension with similarities to yeast Sup35p.
  • The longer form of human Sup35p is the predominant isoform and is conserved across species.
  • Human Sup35p may possess prion-like properties analogous to the yeast [psi] element, impacting translation termination.