Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis

Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2690-5. doi: 10.1073/pnas.052018199. Epub 2002 Feb 26.

Abstract

We present an approach that allows rapid determination of the topology of Escherichia coli inner-membrane proteins by a combination of topology prediction and limited fusion-protein analysis. We derive new topology models for 12 inner-membrane proteins: MarC, PstA, TatC, YaeL, YcbM, YddQ, YdgE, YedZ, YgjV, YiaB, YigG, and YnfA. We estimate that our approach should make it possible to arrive at highly reliable topology models for roughly 10% of the approximately 800 inner-membrane proteins thought to exist in E. coli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase
  • Bacterial Proteins / metabolism*
  • Cyclin-Dependent Kinases / genetics
  • Cyclin-Dependent Kinases / metabolism*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins
  • Genes, Reporter
  • Green Fluorescent Proteins
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Membrane Proteins / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Time Factors

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Luminescent Proteins
  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Cyclin-Dependent Kinases
  • Alkaline Phosphatase
  • phoA protein, E coli