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Genetic study of a membrane protein: DNA sequence alterations due to 17 lamB point mutations affecting adsorption of

J M Clément1, E Lepouce, C Marchal

  • 1Unité de Programmation Moléculaire et Toxicologie Génétique, CNRS LA 271, INSERM U.163, Institut Pasteur, Paris, France.

The EMBO Journal
|January 1, 1983
PubMed

Insights

Researchers identified specific DNA changes in the lamB gene conferring resistance to phage lambda in Escherichia coli. These mutations affect the lambda receptor protein, impacting phage interactions and providing insights into receptor structure.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • The lamB gene in Escherichia coli K12 encodes the outer membrane receptor crucial for phage lambda entry.
  • Bacterial outer membrane proteins play vital roles in cellular processes and interactions with external agents like bacteriophages.

Purpose of the Study:

  • To determine the DNA sequence alterations in lamB conferring resistance to phage lambda.
  • To correlate these mutations with phenotypic classes based on phage growth patterns.
  • To understand the topological organization of the lambda receptor.

Main Methods:

  • DNA sequencing of 17 lamB point mutations.
  • Phenotypic analysis of mutant strains using three different phages (lambda h, lambda hh*, K10).
  • Analysis of missense (Gly to Asp) and nonsense (Trp to amber) mutations.

Main Results:

  • Identified 17 lamB mutations conferring phage lambda resistance.
  • Four phenotypic classes were observed, linked to specific mutation sites.
  • Missense mutations (Gly to Asp) occurred at positions 151, 382, and 401.
  • Nonsense mutations (Trp to amber) occurred at positions 120 and 351.

Conclusions:

  • Specific amino acid changes in the lambda receptor protein are responsible for phage resistance.
  • The identified mutation sites provide insights into the structural and topological organization of the lambda receptor.
  • The limited number of altered sites suggests specific functional regions within the receptor are critical for phage binding.

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