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Effect of heat shock on Rickettsia prowazekii Madrid E from four independent biological replicates

ABSTRACT: Here we present the first microarray analysis of global gene expression changes in the obligate intracytoplasmic pathogen Rickettsia prowazekii using temperature upshift as a model stress condition. We describe a methodology for isolating highly-purified rickettsial RNA where a combination of differential centrifugation and use of Ambion’s MICROBEnrich reagent removed the majority (~90 %) of host cell RNA. A pool of rickettsiae-infected L-cells grown at 34 oC was split and half of the sample was challenged at 42 oC for 30 minutes, total RNA was isolated and converted to cDNA followed by hybridization to an oligonucleotide DNA array. We report data (duplicate hybridizations) from four, independent biological replicates. Twenty-three rickettsial transcripts were significantly increased by temperature upshift greater than two-fold and no transcripts demonstrated reproducible decreases. Notably, the GroESL, DnaK, and DnaJ members of the family of chaperones as well as the two R. prowazekii proteins annotated as putative heat shock proteins were induced. In addition, proteins annotated as proteases were also induced indicating that R. prowazekii mounts a response to heat-shock induced protein unfolding. These data are the first global analysis of the R. prowazekii transcriptome and provide insight into the mechanisms employed by rickettsiae to adapt to temperature upshifts.

ORGANISM(S): Rickettsia prowazekii str. Madrid E

PROVIDER: GSE12377 | GEO | 2008/08/08

SECONDARY ACCESSION(S): PRJNA113123

REPOSITORIES: GEO

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Project description:Proctor2005 - Actions of chaperones and their role in ageing This model is described in the article: Modelling the actions of chaperones and their role in ageing. Proctor CJ, Soti C, Boys RJ, Gillespie CS, Shanley DP, Wilkinson DJ, Kirkwood TB. Mech. Ageing Dev. 2005 Jan; 126(1): 119-131 Abstract: Many molecular chaperones are also known as heat shock proteins because they are synthesised in increased amounts after brief exposure of cells to elevated temperatures. They have many cellular functions and are involved in the folding of nascent proteins, the re-folding of denatured proteins, the prevention of protein aggregation, and assisting the targeting of proteins for degradation by the proteasome and lysosomes. They also have a role in apoptosis and are involved in modulating signals for immune and inflammatory responses. Stress-induced transcription of heat shock proteins requires the activation of heat shock factor (HSF). Under normal conditions, HSF is bound to heat shock proteins resulting in feedback repression. During stress, cellular proteins undergo denaturation and sequester heat shock proteins bound to HSF, which is then able to become transcriptionally active. The induction of heat shock proteins is impaired with age and there is also a decline in chaperone function. Aberrant/damaged proteins accumulate with age and are implicated in several important age-related conditions (e.g. Alzheimer's disease, Parkinson's disease, and cataract). Therefore, the balance between damaged proteins and available free chaperones may be greatly disturbed during ageing. We have developed a mathematical model to describe the heat shock system. The aim of the model is two-fold: to explore the heat shock system and its implications in ageing; and to demonstrate how to build a model of a biological system using our simulation system (biology of ageing e-science integration and simulation (BASIS)). This model is hosted on BioModels Database and identified by: BIOMD0000000091. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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Effect of heat shock on Rickettsia prowazekii Madrid E from four independent biological replicates

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