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Volume 151, Issue 3

Diverse roles for HspR in revealed by the proteome, transcriptome and phenotypic characterization of an mutant Free

Abstract

is a leading cause of bacterial gastroenteritis in the developed world. The role of a homologue of the negative transcriptional regulatory protein HspR, which in other organisms participates in the control of the heat-shock response, was investigated. Following inactivation of in , members of the HspR regulon were identified by DNA microarray transcript profiling. In agreement with the predicted role of HspR as a negative regulator of genes involved in the heat-shock response, it was observed that the transcript amounts of 13 genes were increased in the mutant, including the chaperone genes , and , and a gene encoding the heat-shock regulator HrcA. Proteomic analysis also revealed increased synthesis of the heat-shock proteins DnaK, GrpE, GroEL and GroES in the absence of HspR. The altered expression of chaperones was accompanied by heat sensitivity, as the mutant was unable to form colonies at 44 °C. Surprisingly, transcriptome analysis also revealed a group of 17 genes with lower transcript levels in the mutant. Of these, eight were predicted to be involved in the formation of the flagella apparatus, and the decreased expression is likely to be responsible for the reduced motility and ability to autoagglutinate that was observed for mutant cells. Electron micrographs showed that mutant cells were spiral-shaped and carried intact flagella, but were elongated compared to wild-type cells. The inactivation of also reduced the ability of to adhere to and invade human epithelial INT-407 cells , possibly as a consequence of the reduced motility or lower expression of the flagellar export apparatus in mutant cells. It was concluded that, in , HspR influences the expression of several genes that are likely to have an impact on the ability of the bacterium to successfully survive in food products and subsequently infect the consumer.

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Keyword(s): 2D, two dimensional and HAIR, HspR-associated inverted repeat
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2005-03-01
2024-04-20
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Diverse roles for HspR in Campylobacter jejuni revealed by the proteome, transcriptome and phenotypic characterization of an hspR mutant
Microbiology 151, 905 (2005); https://doi.org/10.1099/mic.0.27513-0
/content/journal/micro/10.1099/mic.0.27513-0
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