Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2003 Jan;47(1):159-69.
doi: 10.1046/j.1365-2958.2003.03264.x.

A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis

Affiliations
Free article

A role for division-site-selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis

Sabine Autret et al. Mol Microbiol. 2003 Jan.
Free article

Abstract

The Bacillus subtilis soj-spo0J locus encodes two proteins belonging to a family of proteins (the ParAB proteins) with dual roles in plasmid or chromosome segregation and transcriptional regulation. Soj protein was previously shown to be capable of abrupt subcellular relocation. The movement was highly co-operative and at any moment, most of the Soj in any cell formed a single large 'patch' covering all or part of one nucleoid. Movement, and co-operativity, in the sense of formation of a single patch, was dependent on Spo0J. Movement, but not co-operativity, was also shown to be dependent, directly or indirectly, on FtsZ protein. We now report that the ftsZ effect arises because jumping onto a nucleoid is promoted by proximity to a cell pole. Studies of other mutants affected in cell division suggest that the attraction to the cell pole is mediated by the division-site-selection protein, MinD (which localizes at the cell poles). It does not require MinC, the main effector of the division site selection system. A mutant form of Soj, putatively locked in the ATP form of the protein, interacts with the cell pole (dependent on MinD) but not with the nucleoid. These results identify a novel function for MinD and demonstrate an intriguing link between proteins involved in the cell division and chromosome segregation machineries.

PubMed Disclaimer

Publication types

MeSH terms

Substances

LinkOut - more resources