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A structural insight into the prokaryotic heat shock transcription regulatory protein ?(32): an implication of ?(32)-DnaK interaction.

ABSTRACT: The heat shock response mechanism is a very vital biochemical process and is mainly controlled by ?(32) protein. The function of ?(32) is temperature dependent and at lower temperatures ?(32) is inactivated by its interactions with DnaK. This interaction is completely abolished above 42°C till date no molecular details of the interactions are available. In the present scenario, an attempt has been made to analyze first the predicted structure of ?(32) obtained by comparative modeling techniques and then to study the interactions between ?(32) and DnaK. From this molecular modeling study we could specifically identify the binding sites of the interactions of ?(32) with DnaK which will enlighten the mechanism of regulation of its activity and stability by DnaK. Our study provides the idea for future mutational experiments in order to find out the possible roles of the amino acids of region2 and region3 of ?(32) in stability as well as in binding with DnaK.

SUBMITTER: Roy SS

PROVIDER: S-EPMC3524887 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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A structural insight into the prokaryotic heat shock transcription regulatory protein σ(32): an implication of σ(32)-DnaK interaction.

Roy Sourav Singha SS Patra Monobesh M Dasgupta Rakhi R Bagchi Angshuman A

Bioinformation 20121031 21

The heat shock response mechanism is a very vital biochemical process and is mainly controlled by σ(32) protein. The function of σ(32) is temperature dependent and at lower temperatures σ(32) is inactivated by its interactions with DnaK. This interaction is completely abolished above 42°C till date no molecular details of the interactions are available. In the present scenario, an attempt has been made to analyze first the predicted structure of σ(32) obtained by comparative modeling techniques ...[more]

PMID: 23275701

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Project description:Cells reprogram their transcriptome in response to stress, such as heat shock. In free-living bacteria, the transcriptomic reprogramming is mediated by increased DNA-binding activity of heat shock sigma factors and activation of genes normally repressed by heat-induced transcription factors. In this study, we performed transcriptomic analyses to investigate heat shock response in the obligate intracellular bacterium Chlamydia trachomatis, whose genome encodes only three sigma factors and a single heat-induced transcription factor. Nearly one-third of C. trachomatis genes showed statistically significant (≥1.5-fold) expression changes 30 min after shifting from 37 to 45°C. Notably, chromosomal genes encoding chaperones, energy metabolism enzymes, type III secretion proteins, as well as most plasmid-encoded genes, were differentially upregulated. In contrast, genes with functions in protein synthesis were disproportionately downregulated. These findings suggest that facilitating protein folding, increasing energy production, manipulating host activities, upregulating plasmid-encoded gene expression, and decreasing general protein synthesis helps facilitate C. trachomatis survival under stress. In addition to relieving negative regulation by the heat-inducible transcriptional repressor HrcA, heat shock upregulated the chlamydial primary sigma factor σ66 and an alternative sigma factor σ28. Interestingly, we show for the first time that heat shock downregulates the other alternative sigma factor σ54 in a bacterium. Downregulation of σ54 was accompanied by increased expression of the σ54 RNA polymerase activator AtoC, thus suggesting a unique regulatory mechanism for reestablishing normal expression of select σ54 target genes. Taken together, our findings reveal that C. trachomatis utilizes multiple novel survival strategies to cope with environmental stress and even to replicate. Future strategies that can specifically target and disrupt Chlamydia's heat shock response will likely be of therapeutic value.

Dataset Information

A structural insight into the prokaryotic heat shock transcription regulatory protein ?(32): an implication of ?(32)-DnaK interaction.

Publications

A structural insight into the prokaryotic heat shock transcription regulatory protein σ(32): an implication of σ(32)-DnaK interaction.

Similar Datasets

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