Secretion of slow-folding proteins by a Type 1 secretion system.

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

Bioengineered

journal_title

Bioengineered

authors

Schwarz CK,Lenders MH,Smits SH,Schmitt L

doi

10.4161/bioe.20712

subject

Has Abstract

pub_date

2012-09-01 00:00:00

pages

289-92

issue

5

eissn

2165-5979

issn

2165-5987

pii

20712

journal_volume

3

pub_type

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