The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes

FEMS Microbiol Rev. 2014 May;38(3):380-92. doi: 10.1111/1574-6976.12045. Epub 2013 Nov 18.


Structural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase 'head' domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization 'hinge'. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation.

Keywords: SMC; chromosome; chromosome organization; chromosome segregation; cohesin; condensin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Chromosomes, Bacterial / chemistry*
  • Chromosomes, Bacterial / metabolism*


  • Bacterial Proteins