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Related Experiment Videos

Structure/function analysis of ras using random mutagenesis coupled with functional screening assays.

L A Feig1, M Corbley, B T Pan

  • 1Dana-Farber Cancer Institute, Boston, Massachusetts.

Molecular Endocrinology (Baltimore, Md.)
|February 1, 1987
PubMed
Summary
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Functional assays for ras proteins (p21) identified mutants affecting guanine nucleotide binding and transforming activity. This research defines key domains of p21 involved in biochemical and biological functions.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The ras protein (p21) plays a crucial role in cellular signaling pathways.
  • Mutations in ras genes are frequently observed in various human cancers.
  • Understanding ras protein function is vital for cancer research and therapeutic development.

Purpose of the Study:

  • To review and detail the application of functional assays for screening ras protein (p21) mutants.
  • To identify ras protein mutants with defects in guanine nucleotide interactions or transforming activity.
  • To characterize these mutants to define functional domains of p21.

Main Methods:

  • Functional assays were employed to assess GTP binding and GTP-dependent autokinase activities directly on bacterial colonies expressing p21.

Related Experiment Videos

  • Random mutagenesis of a v-rasH expression vector and a v-rasH retroviral shuttle vector was performed.
  • NIH cells were infected with mutagenized retroviruses, and nontransformed colonies were isolated to identify transformation-defective mutants.

    • Main Results:

    • Mutant ras genes encoding proteins deficient in GTP binding or GTP-dependent autokinase activity were successfully isolated.
    • Transformation-defective ras mutants were identified and rescued from infected NIH cells.
    • Characterization of isolated mutants provided insights into domains critical for p21's biochemical and biological functions.

    Conclusions:

    • Functional assays are effective tools for screening ras protein mutants.
    • The study defined specific domains of p21 essential for guanine nucleotide binding and transforming activity.
    • This research contributes to understanding the role of guanine nucleotide binding in ras protein function and its implications in disease.