Abstract:
:Protein production through dedicated secretion systems might offer an potential alternative to the conventional cytoplasmical expression. The application of Type 1 secretion systems of Gram-negative bacteria, however, where often not successful in the past for a wide range of proteins. Recently, two studies using the E. coli maltose binding protein (MalE) and the rat intestinal fatty acid binding protein (IFABP) revealed a rational to circumvent these limitations. Here, wild-type passenger proteins were not secreted, while folding mutants with decreased folding kinetics were efficiently exported to the extracellular space. Subsequently, an one-step purification protocol yielded homogeneous and active protein. Taken together, theses two studies suggest that the introduction of slow-folding mutations into a protein sequence might be the key to use Type 1 secretion systems for the biotechnological production of proteins.
journal_name
Bioengineeredjournal_title
Bioengineeredauthors
Schwarz CK,Lenders MH,Smits SH,Schmitt Ldoi
10.4161/bioe.20712subject
Has Abstractpub_date
2012-09-01 00:00:00pages
289-92issue
5eissn
2165-5979issn
2165-5987pii
20712journal_volume
3pub_type
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