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Related Experiment Videos

A polybasic domain allows nonprenylated Ras proteins to function in Saccharomyces cerevisiae

D A Mitchell1, L Farh, T K Marshall

  • 1Department of Biochemistry, University of Iowa, Iowa City 52242.

The Journal of Biological Chemistry
|August 26, 1994
PubMed
Summary
This summary is machine-generated.

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Yeast Ras2 protein function is not solely dependent on the CaaX box motif. Mutations altering posttranslational modifications, like prenylation and palmitoylation, can still yield functional Ras proteins, revealing flexibility in membrane association.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Ras proteins require posttranslational modifications for plasma membrane association.
  • Key modifications include farnesylation, proteolysis, methylesterification, and palmitoylation.
  • The CaaX box motif initiates these modifications via prenyl transferase recognition.

Purpose of the Study:

  • To investigate the functional requirements for Ras membrane association.
  • To assess the role of prenylation, palmitoylation, and basic amino acid stretches in yeast Ras2 protein function.
  • To identify alternative carboxyl-terminal motifs that support Ras protein functionality.

Main Methods:

  • Site-directed mutagenesis of the yeast Ras2 protein CaaX box.
  • Analysis of Ras2 protein function in yeast strains with modified carboxyl-terminal sequences.

Related Experiment Videos

  • Assessment of protein prenylation and palmitoylation status for mutant Ras2 proteins.

    • Main Results:

    • Mutations replacing the CaaX box with a Lys-Leu-Ile-Lys-Arg-Lys sequence encode functional Ras proteins.
    • One mutant, Ras2(CCIIKLIKRK), exhibited wild-type Ras2 function, while Ras2(SCIIKLIKRK) and Ras2(SSIIKLIKRK) showed reduced function at 30°C and thermosensitivity at 37°C.
    • Mutants lacking basic residues (Ras2(CCIISIIS)) were non-functional, and extension mutants were not prenylated, but some were palmitoylated.

    Conclusions:

    • Functional Ras proteins in yeast can be generated by diverse carboxyl-terminal sequences beyond the canonical CaaX box.
    • Posttranslational modifications, including palmitoylation, play crucial roles in Ras protein function, even with altered terminal motifs.
    • This study highlights the adaptability of Ras protein targeting and function through varied modification pathways.