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Escherichia coli proteome analysis using the gene-protein database

R A VanBogelen1, K Z Abshire, B Moldover

  • 1Molecular Biology Department, Parke-Davis Pharmaceutical Research, Division of Warner Lambert Company, Ann Arbor, MI 48105, USA. vanbogr@aa.wl.com

Electrophoresis
|August 1, 1997
PubMed
Summary

The Escherichia coli gene-protein database maps over 1600 proteins using 2-D gel electrophoresis. Ongoing projects aim to fully characterize the E. coli proteome for cell modeling and drug discovery applications.

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Area of Science:

  • Proteomics
  • Genomics
  • Systems Biology

Background:

  • The Escherichia coli gene-protein database compiles data from 2-D polyacrylamide gel electrophoresis.
  • It currently includes approximately 1600 identified protein spots.
  • Data encompasses protein identification and expression levels under various growth conditions.

Purpose of the Study:

  • To further elucidate the Escherichia coli proteome.
  • To map all open reading frames encoded by the E. coli chromosome on 2-D gels.
  • To determine expression conditions, abundance, and cellular location for each protein.

Main Methods:

  • Two-dimensional (2-D) polyacrylamide gel electrophoresis for protein separation.
  • Database compilation of protein identification and expression data.

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  • Ongoing projects focused on proteome characterization.

    • Main Results:

    • The database contains data for about 1600 protein spots from E. coli.
    • Information on protein identification and expression variability is available.
    • Three major projects are underway to comprehensively analyze the proteome.

    Conclusions:

    • The E. coli proteome database is a valuable resource for understanding cellular processes.
    • Applications include cell modeling and therapeutic drug discovery.
    • Further research will provide a more complete proteome map.