Specificity and structural characterization of the PDZ domain from DegS, an extracytoplasmic E. coli protease
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50489670-MIT.pdf
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Author(s)
Walsh, Nathan P.
(Nathan Peter),
1973-
Advisor(s)
Robert T. Sauer.
Date Issued
Invalid Date
Publisher
Massachusetts Institute of Technology
Abstract
DegS is a membrane-bound bacterial protease that is involved in the extracytoplasmic-stress response. The C-terminal domain has limited homology to PDZ domains and was thought to be involved in regulation or substrate recognition. A model of this PDZ domain was generated from NMR solution studies and homology modeling. Peptide selection studies identified the sequence Tyr-Tyr-Phe (YYF) as a C-terminal motif that binds to the PDZ domain. Possible targets were identified including many of the outer-membrane proteins (OMPs), which contain both a conserved terminal YxF and internal YYF sequences. The binding of the DegS PDZ domain to a YYF peptide and OMP derivatives were confirmed using microcalorimetry. Because stress signaling can be triggered by over-expression of some of the outer-membrane proteins, I propose that DegS may receive a signal from unassembled OMPs and transmit it to the aE transcription factor by increasing proteolysis of RseA.
Description
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, February 2002
Includes bibliographical references (p. 87-95).
Subjects
Biology.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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