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Related Experiment Videos

The lethal lambda S gene encodes its own inhibitor.

U Bläsi1, C Y Chang, M T Zagotta

  • 1Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843.

The EMBO Journal
|April 1, 1990
PubMed
Summary
This summary is machine-generated.

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Lambda phage lysis gene S produces two proteins, S105 and S107, affecting cell lysis. S107 inhibits S105, but membrane energization converts S107 into a lysis effector, forming a pore.

Area of Science:

  • Bacteriophage biology
  • Molecular mechanisms of cell lysis
  • Membrane protein function

Background:

  • The lambda phage lysis gene S initiates translation from two start codons, producing S105 and S107 proteins.
  • The differential expression of these proteins impacts the timing and execution of phage-induced cell lysis.
  • A model proposes S107 inhibits S105, the primary lysis effector, despite minor structural differences.

Purpose of the Study:

  • To investigate the in vivo existence and function of S105 and S107 proteins.
  • To elucidate the inhibitory mechanism of S107 on S105.
  • To understand the role of membrane potential in regulating S107 activity and cell lysis.

Main Methods:

  • Immunological detection of S105 and S107 proteins in vivo.

Related Experiment Videos

  • Biochemical assays to characterize protein stability and localization.
  • Analysis of S107 function under varying membrane potential conditions (e.g., using energy poisons).

    • Main Results:

    • Both S105 and S107 are stable, membrane-bound proteins detectable in vivo.
    • S107 functions as a trans-acting inhibitor, with Lys2 residue being critical for this activity.
    • Disruption of membrane energization abolishes S107 inhibition and activates its lysis effector function.

    Conclusions:

    • A two-step model for gene S-mediated lysis is proposed, involving protein accumulation and pore formation.
    • Lateral diffusion of S monomers within membrane patches is crucial for pore formation.
    • Membrane energization state regulates the transition from S107 inhibition to lysis effector activity.