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Cloned DNA fragment specifying major outer membrane protein a in Escherichia coli K-12

Journal of Bacteriology
|October 1, 1978
PubMed

Insights

Recombinant plasmid pMC44 produces a unique outer membrane protein (M2) in Escherichia coli. This protein M2 is identical to a major outer membrane protein found in normal E. coli K-12.

Area of Science:

  • Molecular Biology
  • Bacteriology
  • Genetics

Background:

  • Recombinant plasmids are crucial tools for studying gene function and protein expression.
  • Understanding bacterial outer membrane proteins is vital for drug development and pathogenesis research.

Purpose of the Study:

  • To identify and characterize polypeptides encoded by the recombinant plasmid pMC44.
  • To determine which of these polypeptides are unique to pMC44 compared to its parent plasmid pSC101.
  • To ascertain the cellular localization and abundance of novel polypeptides.

Main Methods:

  • Construction of recombinant plasmid pMC44 by joining an E. coli K-12 DNA fragment to pSC101.
  • Analysis of polypeptides synthesized by pMC44 and pSC101 in minicells.
  • Fractionation of cell envelope components using Sarkosyl treatment.
  • Identification and comparison of Sarkosyl-insoluble and Sarkosyl-soluble membrane proteins.

Main Results:

  • Plasmid pMC44 specifies three unique polypeptides.
  • One polypeptide, M2, is a Sarkosyl-insoluble outer membrane protein encoded by the cloned E. coli DNA fragment.
  • M2 is synthesized in quantities comparable to abundant E. coli K-12 outer membrane proteins.
  • Evidence suggests M2 is the native E. coli outer membrane protein 'a' (Lugtenberg) or '3b' (Schnaitman).

Conclusions:

  • The recombinant plasmid pMC44 facilitates the expression of a specific E. coli outer membrane protein.
  • This study identifies a key outer membrane protein and provides a tool for its further investigation.
  • The findings contribute to understanding the genetic basis and production of essential bacterial outer membrane proteins.

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