Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli.
The cell envelope of Gram-negative bacteria is a complex macromolecular structure that is essential for their viability. Little is known on how the proteins which are secreted to the envelope fold into their unique three-dimensional structure. Several folding factors, including chaperones and protein folding catalysts involved in disulfide bond formation, have been identified in the periplasm. The characterization of these proteins has advanced our understanding of envelope biogenesis, although many fundamental questions remain unanswered. In particular, we still do not know how beta-barrel proteins are transported through the periplasm and inserted into the outer membrane. Here, we discuss the recent discoveries that have shed new light on the mechanisms that ensure the correct folding of envelope proteins. We have paid particular attention to the significant contribution of proteomic studies.
Leverrier
Pauline
P
de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Vertommen
Didier
D
Collet
Jean-François
JF
D002473:Cell Wall / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000096:biosynthesis*; D017510:Protein Folding; D040901:Proteomics
D029968:Escherichia coli Proteins