AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cha, H. J.
Right arrow Articles by Bentley, W. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cha, H. J.
Right arrow Articles by Bentley, W. E.
Agricola
Right arrow Articles by Cha, H. J.
Right arrow Articles by Bentley, W. E.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 1999, p. 409-414, Vol. 65, No. 2
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Green Fluorescent Protein as a Noninvasive Stress Probe in Resting Escherichia coli Cells

Hyung Joon Cha,1,2 Ranjan Srivastava,1,2 Vikram N. Vakharia,1 Govind Rao,3 and William E. Bentley1,2,*

Center for Agricultural Biotechnology, University of Maryland Biotechnology Institute, College Park, Maryland 20742,1 Department of Chemical Engineering, University of Maryland, College Park, Maryland 20742,2 and Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore County, Baltimore, Maryland 212503

Received 28 July 1998/Accepted 4 November 1998

We constructed and characterized three stress probe plasmids which utilize a green fluorescent protein as a noninvasive reporter in order to elucidate Escherichia coli cellular stress responses in quiescent or resting cells. Cellular stress levels were easily detected by fusing three heat shock stress protein promoter elements, those of the heat shock transcription factor sigma 32, the protease subunit ClpB, and the chaperone DnaK, to the reporter gene gfpuv. When perturbed by a chemical or physical stress (such as a heat shock, nutrient [amino acid] limitation, or addition of IPTG [isopropyl-beta -D-thiogalactopyranoside], acetic acid, ethanol, phenol, antifoam, or salt [osmotic shock]), the E. coli cells produced GFPuv, which was easily detected within the cells as emitted green fluorescence. Temporal and amplitudinal mapping of the responses was performed, and the results revealed regions where quantitative delineation of cell stress was afforded.

* Corresponding author. Mailing address: Department of Chemical Engineering, University of Maryland, College Park, MD 20742. Phone: (301) 405-4321. Fax: (301) 314-9075. E-mail: bentley{at}eng.umd.edu.

Applied and Environmental Microbiology, February 1999, p. 409-414, Vol. 65, No. 2
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 1999 by the American Society for Microbiology. All rights reserved.