The Traxler Lab is doing research on Escherichia coli, the best understood organism in the world. Below are provided links that will allow you to order cultures, search databases and find articles on E. coli.
Our Research in the Traxler Lab |
The focus of Dr. Traxler's lab is the genetic and biochemical analysis of
membrane protein folding. The lab is examining two different models systems,
both found in the cytoplasmic membrane of the Gram negative bacterium
Escherichia coli. One ongoing project uses proteins involved in maltose
transport as an example of the in vivo folding process for heteromeric membrane
protein complexes in general and for proteins of the ATP-binding cassette
superfamily in particular. Other related proteins in this broadly distributed
and highly conserved family include the bacterial binding protein-dependent
transporters and the CFTR protein which is defective in humans with cystic
fibrosis.
The maltose transporter contains 4 subunits: 1 molecule of MalF, 1 of MalG, and
2 of MalK. One set of studies addresses how the proteins are localized to the
membrane prior to complex assembly. Once the proteins have been properly
targeted to the membrane, mutational analyses are helping the lab to define how
the protein subunits recognize one another and oligomerize within the plane of
the membrane. Biochemical studies exploiting this collection of mutants are
focused on defining the assembly pathway for the complex.
A second project in the lab focuses on the membrane-based events during late
stages of bacterial conjugation. Bacterial conjugation is an efficient way to
transfer genetic information among prokaryotes and accounts for the
dissemination of many antibiotic resistance determinants among pathogens. The
analysis exploits the well characterized F plasmid of E. coli as a model and
aims to characterize the mechanism of DNA transfer through the cell envelope.
Only one F plasmid-encoded protein, TraD, seems to act specifically during the
DNA transfer stage of conjugation. Several other conjugal plasmids encode
homologs of TraD. Structure-function studies with TraD and some of its homologs
will be used to model the activities of these proteins during DNA transfer.
The UW Department of Microbiology
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