Streptomyces coelicolor Dps-like proteins: differential dual roles in response to stress during vegetative growth and in nucleoid condensation during reproductive cell division

The Dps protein, a member of the ferritin family, contributes to DNA protection during oxidative stress and plays a central role in nucleoid condensation during stationary phase in unicellular eubacteria. Genome searches revealed the presence of three Dps-like orthologues within the genome of the Gr...

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Bibliographic Details
Published in:Molecular microbiology Vol. 73; no. 6; pp. 1186 - 1202
Main Authors: Facey, P.D, Hitchings, M.D, Saavedra-Garcia, P, Fernandez-Martinez, L, Dyson, P.J, Del Sol, R
Format: Journal Article
Language:English
Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01-09-2009
Blackwell Publishing Ltd
Blackwell
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Summary:The Dps protein, a member of the ferritin family, contributes to DNA protection during oxidative stress and plays a central role in nucleoid condensation during stationary phase in unicellular eubacteria. Genome searches revealed the presence of three Dps-like orthologues within the genome of the Gram-positive bacterium Streptomyces coelicolor. Disruption of the S. coelicolor dpsA, dpsB and dpsC genes resulted in irregular condensation of spore nucleoids in a gene-specific manner. These irregularities are correlated with changes to the spacing between sporulation septa. This is the first example of these proteins playing a role in bacterial cell division. Translational fusions provided evidence for both developmental control of DpsA and DpsC expression and their localization to sporogenic compartments of aerial hyphae. In addition, various stress conditions induced expression of the Dps proteins in a stimulus-dependent manner in vegetative hyphae, suggesting stress-induced, protein-specific protective functions in addition to their role during reproductive cell division. Unlike in other bacteria, the S. coelicolor Dps proteins are not induced in response to oxidative stress.
Bibliography:http://dx.doi.org/10.1111/j.1365-2958.2009.06848.x
Authors contributed equally.
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ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2009.06848.x