title: Improving protein secretion by engineering components of the bacterial translocation machinery.
abstract: The increased insight into the mechanism of bacterial protein translocation has resulted in new concepts for the production of heterologous proteins. The periplasm of gram-negative bacteria is revealed to have a role as a 'protein construction compartment', which can be used to fold complex proteins. Passage across the outer membrane, however, remains a challenge due to the high selectivity of the outer membrane translocase. In gram-positive bacteria, slow folding at the membrane-cell-wall interface can make heterologous proteins vulnerable to degradation by wall-associated proteases. The recent identification of thiol-disulfide oxidoreductases in Bacillus subtilis might open the possibility of secreting proteins containing multiple disulfide bonds from this host.
authors.affiliation: Pharmaceutical Biology, University Centre for Pharmacy, Antonius Deusinglaan 1, 9713, AV Groningen, The Netherlands.
authors.forename: P
authors.initials: P
authors.lastname: Braun
authors.forename: G
authors.initials: G
authors.lastname: Gerritse
authors.forename: J M
authors.initials: JM
authors.lastname: van Dijl
authors.forename: W J
authors.initials: WJ
authors.lastname: Quax
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001693:Biological Transport, Active; D001709:Biotechnology; D002462:Cell Membrane / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000235:genetics / Q000378:metabolism; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones