Architectural organization in E. coli nucleoid

Biochim Biophys Acta. 2012 Jul;1819(7):830-5. doi: 10.1016/j.bbagrm.2012.02.012. Epub 2012 Feb 22.

Abstract

In contrast to organized hierarchical structure of eukaryotic chromosome, bacterial chromosomes are believed not to have such structures. The genomes of bacteria are condensed into a compact structure called the nucleoid. Among many architectural, histone-like proteins which associate with the chromosomal DNA is HU which is implicated in folding DNA into a compact structure by bending and wrapping DNA. Unlike the majority of other histone-like proteins, HU is highly conserved in eubacteria and unique in its ability to bind RNA. Furthermore, an HU mutation profoundly alters the cellular transcription profile and consequently has global effects on physiology and the lifestyle of E. coli. Here we provide a short overview of the mechanisms by which the nucleoid is organized into different topological domains. We propose that HU is a major player in creating domain-specific superhelicities and thus influences the transcription profile from the constituent promoters. This article is part of a Special Issue entitled: Chromatin in time and space.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Chromosomes, Bacterial / genetics*
  • Chromosomes, Bacterial / ultrastructure
  • DNA Packaging
  • DNA, Bacterial / genetics
  • DNA, Bacterial / ultrastructure
  • DNA, Superhelical / genetics
  • DNA, Superhelical / ultrastructure
  • DNA-Binding Proteins / metabolism
  • DNA-Binding Proteins / physiology
  • Escherichia coli / genetics*
  • Escherichia coli / ultrastructure
  • Escherichia coli Proteins / metabolism
  • Escherichia coli Proteins / physiology
  • Insulator Elements
  • Nucleic Acid Conformation
  • RNA, Bacterial / genetics

Substances

  • DNA, Bacterial
  • DNA, Superhelical
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • RNA, Bacterial
  • hns protein, E coli