Affordable Access

Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli.

Authors
  • Han, Mee-Jung
  • Park, Si Jae
  • Park, Tae Jung
  • Lee, Sang Yup
Type
Published Article
Journal
Biotechnology and bioengineering
Publication Date
Nov 20, 2004
Volume
88
Issue
4
Pages
426–436
Identifiers
PMID: 15382106
Source
Medline
License
Unknown

Abstract

Proteome profiling of the inclusion body (IB) fraction of recombinant proteins produced in Escherichia coli suggested that two small heat shock proteins, IbpA and IbpB, are the major proteins associated with IBs. In this study, we demonstrate that IbpA and IbpB facilitate the production of recombinant proteins in E. coli and play important roles in protecting recombinant proteins from degradation by cytoplasmic proteases. We examined the cytosolic production, and Tat- or Sec-dependent secretion of the enhanced green fluorescent protein (EGFP) in wild type, ibpAB(-) mutant, and ibpAB-amplified E. coli strains. Analysis of fluorescence histograms and confocal microscopic imaging revealed that over-expression of the ibpA and/or ibpB genes enhanced cytosolic EGFP production whereas knocking out the ibpAB genes enhanced secretory production. This strategy seems to be generally applicable as it was successfully employed for the enhanced cytosolic or secretory production of several other recombinant proteins in E. coli.

Report this publication

Statistics

Seen <100 times