Robert E. Webster
Professor Emeritus of Biochemistry
Our laboratory is investigating the assembly and function of macromolecular structures associated with the membrane. Presently, two systems are being studied. The first is the Tol protein complex, encoded by the tol QRAB gene, which functions to maintain the integrity of the outer membrane. A class of bacterial toxins, the group A colicins, as well as the conjugative pious specific filamentous bacteriophage also require the Tol protein complex to gain entrance to the bacteria. Problems being addressed are the mechanism of synthesis and translocation of the proteins into the membrane, the mechanism by which these molecules associate into a functional complex and the role this complex plays in the assembly and maintenance of the outer membrane.
The second system is the membrane associated assembly of the class I filamentous bacteriophage fl, M13 and fd. Studies are centered on determining the role that the phage encoded inner membrane assembly proteins, pI and pI*, play in forming the assembly site and how it helps facilitate the assembly of capsid proteins around the DNA. These investigations should help us understand the fundamental principles of membrane associated macromolecular assembly.
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