PMID- 17974510
OWN - NLM
STAT- MEDLINE
DCOM- 20080304
LR  - 20191210
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1774
IP  - 12
DP  - 2007 Dec
TI  - Transport proteins PotD and Crr of Escherichia coli, novel fusion partners for 
      heterologous protein expression.
PG  - 1536-43
AB  - The Escherichia coli proteome response to the stressor GdnHCl was analyzed 
      through 2-dimensional gel electrophoresis (2-DE). We identified PotD 
      (spermidine/putrescine-binding periplasmic protein) and Crr [glucose-specific 
      phosphotransferase (PTS) enzyme IIA component] as a stress-responsive protein. 
      Even under a stress situation where the total number of soluble proteins 
      decreased by about 10%, 3.5- and 2.2-fold increase was observed in the synthesis 
      of PotD and Crr, respectively. As fusion partners, PotD and Crr dramatically 
      increased the solubility of many aggregation-prone heterologous proteins [e.g. 
      human minipro-insulin (mp-INS), human epidermal growth factor (EGF), human 
      prepro-ghrelin (ppGRN), human interleukin-2(hIL-2), human activation induced 
      cytidine deaminase (AID), human glutamate decarboxylase (GAD(448-585)), 
      Pseudomonas putida cutinase (CUT), human ferritin light chain (hFTN-L), human 
      granulocyte colony-stimulating factor (G-CSF), and cold autoinflammatory 
      syndrome1 protein (NALP3) Nacht domain (NACHT)] in the E. coli cytoplasm. 
      Presumably PotD and Crr were very effective in shielding interactive surfaces of 
      heterologous proteins associated with non-specific protein-protein interactions 
      leading to the formation of inclusion bodies most likely due to intrinsic high 
      folding efficiency, chaperone-like activity, or a combination of both factors. 
      Both the stress-induced proteins were well suited for the production of a 
      biologically active fusion mutant of P. putida cutinase that can be expected to 
      be of biotechnological and commercial interest.
FAU - Han, Kyung-Yeon
AU  - Han KY
AD  - Department of Chemical and Biological Engineering, Korea University, Anam-Dong 
      5-1, Sungbuk-Ku, Seoul 136-713, South Korea.
FAU - Seo, Hyuk-Seong
AU  - Seo HS
FAU - Song, Jong-Am
AU  - Song JA
FAU - Ahn, Keum-Young
AU  - Ahn KY
FAU - Park, Jin-Seung
AU  - Park JS
FAU - Lee, Jeewon
AU  - Lee J
LA  - eng
PT  - Evaluation Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20071004
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Periplasmic Binding Proteins)
RN  - 0 (PotD protein, E coli)
RN  - 0 (Proteome)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (crr protein, E coli)
RN  - EC 2.7.1.- (Phosphoenolpyruvate Sugar Phosphotransferase System)
RN  - EC 3.1.1.- (Carboxylic Ester Hydrolases)
RN  - EC 3.1.1.- (cutinase)
SB  - IM
MH  - Carboxylic Ester Hydrolases/genetics/metabolism
MH  - Cloning, Molecular
MH  - Escherichia coli/*genetics
MH  - Escherichia coli Proteins/*genetics/metabolism
MH  - *Gene Expression Regulation
MH  - Inclusion Bodies/metabolism
MH  - Membrane Transport Proteins/*genetics/metabolism
MH  - Periplasmic Binding Proteins/*genetics/metabolism
MH  - Phosphoenolpyruvate Sugar Phosphotransferase System/*genetics/metabolism
MH  - Protein Transport/genetics
MH  - Proteome/analysis
MH  - Pseudomonas putida/genetics
MH  - Recombinant Fusion Proteins/*genetics/metabolism
MH  - *Transduction, Genetic
EDAT- 2007/11/03 09:00
MHDA- 2008/03/05 09:00
CRDT- 2007/11/03 09:00
PHST- 2007/06/02 00:00 [received]
PHST- 2007/09/08 00:00 [revised]
PHST- 2007/09/24 00:00 [accepted]
PHST- 2007/11/03 09:00 [pubmed]
PHST- 2008/03/05 09:00 [medline]
PHST- 2007/11/03 09:00 [entrez]
AID - S1570-9639(07)00247-6 [pii]
AID - 10.1016/j.bbapap.2007.09.012 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2007 Dec;1774(12):1536-43. doi: 
      10.1016/j.bbapap.2007.09.012. Epub 2007 Oct 4.