Protein Folding in Bacteria
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Group Leader Jean-François Collet Contact Jean-François Collet de Duve Institute and Université catholique de Louvain BCHM-GRM - B1.75.08, Avenue Hippocrate 75, B-1200 Brussels phone: 32 (0)2 764 75 62 fax: 32 (0)2 764 74 98 e-mail: Jean-François Collet Group members > |
Our lab is part of The Brussels Center For Redox Biology. The center results from a collaboration between our group and the group of Joris Messens at the Flanders Institute for Biotechnology (VIB, Vrije Universiteit Brussel). Both groups are in Brussels, located 10 minutes apart from each other. The Center benefits from a combined expertise in biochemistry, structural biology and microbiology. We investigate proteins that are involved in thiol-based catalysis mechanisms and oxidative protein folding. We address questions regarding the specificity and promiscuity of the thioredoxin-fold.
Research topics
To be active and stable, newly synthesized proteins have to fold correctly. However, reaching a proper three-dimensional structure is a real challenge. This is especially true for proteins that are secreted to the cell envelope of Gram-negative bacteria. These proteins are assembled in the cytoplasm, are then transported across the inner-membrane and finally fold within the periplasm or the outer-membrane, in an environment devoid of any obvious energy source. Moreover, the correct folding of many of these proteins requires the formation of a disulfide bond between two cysteine residues, which is a rate-limiting step of the folding process.
Failure to fold secreted proteins properly will affect the integrity of the bacterial cell envelope, which will increase the sensitivity of bacteria to antimicrobial drugs.
In our lab, we study the pathways that govern disulfide bond formation in the periplasm of Escherichia coli and the assembling of the bacterial outer-membrane.
