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| Attached Files |
| Name |
Description |
MIMEType |
Size |
Downloads |
JoeReedPresentation.pdf
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JoeReedPresentation.pdf |
application/pdf |
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0 |
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| Title |
Localization of the PilZ domain from the BcsA protein within Escherichia coli
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| Type of Resource |
still image
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| Date Created |
2008-04-23
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| Digital Origin |
born digital
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| Rights Statement |
http://digital.uwyo.edu/copyright.htm
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| Keyword (topic) |
TBD
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| Series Title |
Undergrauate Research Day 2008
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| Creator(s) |
Reed, Joseph M
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| Genre |
Powerpoint/Pdf
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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 |
Recently, cyclic dimeric guanosine monophosphate, c-di-GMP, was shown to function as a novel bacterial second messenger. High concentrations of c-di-GMP cause the formation of biofilm due to synthesis of adhesive surface organelles like pili and production of cellulose causing suppressed motility. In contrast, low c-di-GMP concentrations inhibited biofilm formation and improved motility. C-di-GMP affects virulence in several bacterial pathogens; however, how c-di-GMP affects virulence remains unknown. The Gomelsky lab identified two PilZ receptors, which bind c-di-GMP in Escherichia coli, BcsA and YcgR. YcgR is a soluble protein that the Gomelsky lab has recently shown to be localized in the periplasm. The other receptor is in the bacterial cellulose synthase, BcsA, which is a trans-membrane protein. The PilZ domain located on BcsA binds c-di-GMP. BcsA is woven into the cytoplasmic membrane and crosses from the cytoplasm to the periplasm and back many times. Some computational predictions suggest that the PilZ domain of BcsA is located in the cytoplasm, while others suggest that this domain is located in the periplasm. The purpose of this study was to examine whether the PilZ domain from the BcsA protein is located in the periplasm or the cytoplasm. This would provide important clues as to where c-di-GMP action takes place.
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| Notes |
From - Undergraduate Research Day 2008 - Celebration of Research - Abstracts
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