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Title: Global Analysis of Heat Shock Response in Desulfovibrio vulgaris Hildenborough.

Journal Article · · Journal of Bacteriology
OSTI ID:923002

Desulfovibrio vulgaris Hildenborough belongs to a class ofsulfate-reducing bacteria (SRB) and is found ubiquitously in nature.Given the importance of SRB-mediated reduction for bioremediation ofmetal ion contaminants, ongoing research on D. vulgaris has been in thedirection of elucidating regulatory mechanisms for this organism under avariety of stress conditions. This work presents a global view of thisorganism's response to elevated growth temperature using whole-celltranscriptomics and proteomics tools. Transcriptional response (1.7-foldchange or greater; Z>1.5) ranged from 1,135 genes at 15 min to 1,463genes at 120 min for a temperature up-shift of 13oC from a growthtemperature of 37oC for this organism and suggested both direct andindirect modes of heat sensing. Clusters of orthologous group categoriesthat were significantly affected included posttranslationalmodifications; protein turnover and chaperones (up-regulated); energyproduction and conversion (down-regulated), nucleotide transport,metabolism (down-regulated), and translation; ribosomal structure; andbiogenesis (down-regulated). Analysis of the genome sequence revealed thepresence of features of both negative and positive regulation whichincluded the CIRCE element and promoter sequences corresponding to thealternate sigma factors ?32 and ?54. While mechanisms of heat shockcontrol for some genes appeared to coincide with those established forEscherichia coli and Bacillus subtilis, the presence of unique controlschemes for several other genes was also evident. Analysis of proteinexpression levels using differential in-gel electrophoresis suggestedgood agreement with transcriptional profiles of several heat shockproteins, including DnaK (DVU0811), HtpG (DVU2643), HtrA (DVU1468), andAhpC (DVU2247). The proteomics study also suggested the possibility ofposttranslational modifications in the chaperones DnaK, AhpC, GroES(DVU1977), and GroEL (DVU1976) and also several periplasmic ABCtransporters.

Research Organization:
COLLABORATION - Collaboration with BiosystemsResearch Department Sandia National Laboratory; Environmental SciencesDivision, Oak Ridge National Laboratory; Physical Biosciences Division,Lawrence Be
Sponsoring Organization:
USDOE
DOE Contract Number:
DE-AC02-05CH11231
OSTI ID:
923002
Report Number(s):
LBNL-60298; JOBAAY; TRN: US200804%%833
Journal Information:
Journal of Bacteriology, Vol. 188, Issue 5; Related Information: Journal Publication Date: 2006; ISSN 0021-9193
Country of Publication:
United States
Language:
English