Localization of the PilZ domain from the BcsA ...

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Localization of the PilZ domain from the BcsA protein within Escherichia coli

Name:Personal
Reed, Joseph M
Role :Text(marcrelator)
creator

Name:Personal
Department of Molecular Biology; Dr. Mark Gomelsky
Role :Text(marcrelator)
contributor

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still image
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Powerpoint/Pdf
Origin Information Place
Laramie, Wyoming

University of Wyoming
(keyDate="yes")
2008-04-23

Language:Text
eng

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abstract
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.
note
From - Undergraduate Research Day 2008 - Celebration of Research - Abstracts
Subject
TBDBacteria--Ultrastructure; Molecular microbiology

Related Item:series Title Information
Undergrauate Research Day 2008

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http://digital.uwyo.edu/copyright.htm
Record Information languageOfCataloging :Text(ISO639-2B)
English
:Code(ISO639-2B)
eng