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
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.
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