(has links) (PDF)
Halle, Wittenberg, University, Diss., 2001.
Comparison of the mechanism of transmembrane signaling in bacterial chemoreceptors and sensor kinasesWard, Scott Michael 30 October 2006 (has links)
Membrane-bound receptors transmit information from the cell exterior to the cell interior. Bacterial receptors capable of transmitting this information include sensor kinases, which control gene expression via response regulators, and methyl-accepting chemotaxis proteins (MCPs), which control rotation of the flagellar motor. These receptors, which have a similar general architecture and function, are predicted to share similar mechanisms of transmembrane signaling. The majority of such work has been conducted on MCPs. Our goal is to extend this work to the closely related sensor kinases by creating functional hybrid transducers. I show that a chimeric protein (Nart) that joins the periplasmic, ligandbinding domain of the sensor kinase NarX (nitrate/nitrite sensor) to the cytoplasmic signaling domain of the chemoreceptor Tar is capable of modulating flagellar rotation in response to both nitrate and nitrite. Consistent with the properties of NarX, our Nart elicits a stronger response to nitrate than to nitrite. Introduction of mutations into a highly conserved periplasmic region affects Nart signaling in a fashion that is consistent with the effects seen in NarX. I also present the first example of a substitution in a presumed ligand-binding domain that confers a reverse-signal phenotype for both nitrate and nitrite in Nart. These results support the hypothesis that the key aspects of transmembrane signaling are closely similar in homodimeric bacterial chemoreceptors and sensor kinases.
Warren, Anna Victoria
No description available.
McIntyre, John Malcolm
iv, 125 leaves : ill., appendix / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.)--University of Adelaide, Dept. of Microbiology, 1971
McIntyre, John Malcolm.
(has links) (PDF)
Thesis (Ph.D.) -- University of Adelaide, Dept. of Microbiology, 1971.
Kanemoto, Roy Haruo.
Thesis (M.S.)--University of Wisconsin--Madison, 1982. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 73-77).
Kleene, Steven James.
Thesis (Ph. D.)--University of Wisconsin--Madison, 1980. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
Thesis (doctoral)--Rijksuniversiteit te Utrecht, 1919. / Bibliography: p. - 80.
Daniel, Michael Anthony.
Thesis (Ph. D.)--University of Rochester, 1998. / eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
16 August 2006
The transmembrane serine receptor Tsr associates with a coupling protein, CheW, and a histidine kinase, CheA, to form a ternary complex that regulates the activity of CheA. CheA activity is inhibited by binding of L-serine to Tsr. This work aims to characterize the ligand-binding properties of Tsr and the inhibitory effect of L-serine on CheA activity. The periplasmic domain of Tsr (pTsr) was purified and characterized. Analytical gel filtration and analytical ultracentrifugation indicated that binding of Lserine promotes dimerization. The binding stoichiometry and dissociation constant for binding of L-serine to pTsr were determined by fluorescence spectroscopy. As protein concentration decreased, the dissociation constant increased. A working model was proposed to account for the interactions between L-serine and pTsr. The activity of CheA in a ternary complex with full-length Tsr and CheW was analyzed by measuring the production of [32P]-phospho-CheY. (Phospho-CheY is the product of CheA catalysis.) The results revealed that binding of L-serine decreased CheA activity without changing its affinity for ATP. These findings suggest that the allosteric effect of L-serine on CheA activity might occur through V-type inhibition. Optimization of an alternative, continuous, non-radioactive assay for CheA is underway.
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