Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy

Nucleic Acids Res. 2004 Apr 1;32(6):1982-92. doi: 10.1093/nar/gkh512. Print 2004.

Abstract

A small container of several to a few hundred microm3 (i.e. bacterial cells and eukaryotic nuclei) contains extremely long genomic DNA (i.e. mm and m long, respectively) in a highly organized fashion. To understand how such genomic architecture could be achieved, Escherichia coli nucleoids were subjected to structural analyses under atomic force microscopy, and found to change their structure dynamically during cell growth, i.e. the nucleoid structure in the stationary phase was more tightly compacted than in the log phase. However, in both log and stationary phases, a fundamental fibrous structure with a diameter of approximately 80 nm was found. In addition to this '80 nm fiber', a thinner '40 nm fiber' and a higher order 'loop' structure were identified in the log phase nucleoid. In the later growth phases, the nucleoid turned into a 'coral reef structure' that also possessed the 80 nm fiber units, and, finally, into a 'tightly compacted nucleoid' that was stable in a mild lysis buffer. Mutant analysis demonstrated that these tight compactions of the nucleoid required a protein, Dps. From these results and previously available information, we propose a structural model of the E.coli nucleoid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / physiology
  • Cell Division
  • Cell Nucleus Structures / ultrastructure*
  • Chromosomes, Bacterial / ultrastructure
  • DNA Packaging
  • Escherichia coli / cytology
  • Escherichia coli / genetics
  • Escherichia coli / ultrastructure*
  • Escherichia coli Proteins / physiology
  • Microscopy, Atomic Force

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • dps protein, E coli