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Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli
Author(s) -
Leverrier Pauline,
Vertommen Didier,
Collet JeanFrançois
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900461
Subject(s) - periplasmic space , biogenesis , cell envelope , proteomics , folding (dsp implementation) , protein folding , envelope (radar) , biology , microbiology and biotechnology , chaperone (clinical) , proteome , bacterial outer membrane , computational biology , escherichia coli , chemistry , biochemistry , computer science , medicine , telecommunications , radar , pathology , electrical engineering , gene , engineering
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 β‐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.