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| Title |
A Matter of Life and Death: The search for a c-di-GMP binding partner that allows wild type Escherichia coli to survive while strain BL21 cannot.
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| Type of Resource |
still image
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| Date Created |
2009-05-15
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| Digital Origin |
born digtal
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| Rights Statement |
http://digital.uwyo.edu/copyright.htm
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| Keyword (topic) |
Cyclic dimeric guanosine monophosphate (c-di-GMP)
Escherichia. coli
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| Series Title |
Undergrauate Research Day 2009
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| Creator(s) |
Reed, Joseph M
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| Contributor(s) |
Gomelsky, Dr. Mark
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| Publisher |
University of Wyoming
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| Place of publication |
Laramie, Wyoming
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| Language |
eng
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| Summary |
Cyclic dimeric guanosine monophosphate (c-di-GMP) has been found to be ubiquitous in bacteria. There are two proteins that control the levels of c-di-GMP within the cell; GGDEF domain proteins synthesize c-di-GMP while EAL domain proteins degrade c-di-GMP. The Gomelsky lab has recently shown that overexpression of the GGDEF domain is toxic to Escherichia. coli BL21. When the same GGDEF domain is overexpressed in wild type E. coli the cells grow and express the normal phenotype. Currently there are only two known c-di-GMP binding partners in E. coli, PilZ and YcgR domains. We hypothesize that E. coli BL21, which contains both PilZ and YcgR protein domains, is missing another unknown c-di-GMP binding partner that would allow for its survival in the presence of elevated amounts of c-di-GMP. To find this new c-di-GMP binding partner we successfully created a wild type E. coli genome library and introduced it into the BL21 strain overexpressing the GGDEF protein domain. We have collected 18 colonies that survived; among them three colonies have an unidentified gene that we are currently analyzing.
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| Notes |
From - Undergraduate Research Day 2009 - Celebration of Research - Abstracts
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