Expression of the fusion protein between protein A and the transit peptide of the small subunit of ribulose 1,5-bisphosphate carboxylase in Escherichia coli

1987 ◽  
Vol 15 (6) ◽  
pp. 1143-1144
Author(s):  
N. KADERBHAI ◽  
R. B. BEECHEY ◽  
A. EVANS ◽  
M. HE ◽  
M. A. KADERBHAI
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Protein A ◽  
Transit Peptide ◽  
Small Subunit ◽  
Bisphosphate Carboxylase

scholarly journals Fibroblast adhesion to recombinant tropoelastin expressed as a protein A-fusion protein

1991 ◽  
Vol 273 (3) ◽  
pp. 517-522 ◽  
Author(s):  
L E Grosso ◽  
W C Parks ◽  
L J Wu ◽  
R P Mecham
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Fusion Protein ◽  
Developmental Regulation ◽  
Protein A ◽  
Receptor Binding Site ◽  
Elastin Receptor ◽  
Cnbr Cleavage ◽  
Fibroblast Adhesion ◽  
Nuchal Ligament

A bovine tropoelastin cDNA encoding exons 15-36 that includes the elastin-receptor binding site was expressed in Escherichia coli as a fusion protein with Protein A from Staphylococcus aureus. After isolation of the fusion protein by affinity chromatography on Ig-Sepharose, the tropoelastin domain was separated from plasmid-pR1T2T-encoded Protein A (Protein A') by CNBr cleavage. Cell-adhesion assays demonstrated specific adhesion to the recombinant tropoelastin. Furthermore, the data indicate that interactions involving the bovine elastin receptor mediate nuchalligament fibroblast adhesion to the recombinant protein. In agreement with earlier studies of fibroblast chemotaxis to bovine tropoelastin, nuchal-ligament fibroblast adhesion demonstrated developmental regulation of the elastin receptor.

Expression of recombinant human glucose-dependent insulinotropic polypeptide in Escherichia coli by sequence-specific proteolysis of a protein A fusion protein

Peptides ◽  
1990 ◽  
Vol 11 (6) ◽  
pp. 1069-1074 ◽  
Author(s):  
Billy K.-C. Chow ◽  
Glenn W. Morrow ◽  
Margaret Ho ◽  
Raymond A. Pederson ◽  
Christopher H.S. McIntosh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Protein A

Use of chimaeric genes harbouring small subunit transit peptide sequences to study transport in chloroplasts

1986 ◽  
Vol 313 (1162) ◽  
pp. 429-432 ◽  
Keyword(s):  
High Efficiency ◽  
Transit Peptide ◽  
Small Subunit ◽  
Peptide Sequence ◽  
Ribulose Bisphosphate Carboxylase ◽  
Bisphosphate Carboxylase ◽  
Quantitative Measurements ◽  
Marker Proteins ◽  
Necessary And Sufficient

A sequence coding for the transit peptide part of the precursor of the ribulose bisphosphate carboxylase small subunit can be used to construct chimaeric genes coding for easily detectable marker proteins. Chloroplasts of transgenic plants containing such chimaeric genes were found to contain the marker proteins. In addition, measurements of uptake by isolated chloroplasts of various precursor proteins, synthesized in vitro , demonstrated that most if not all of the transit peptide sequence was necessary and sufficient to obtain transport into chloroplasts. However, quantitative measurements of uptake indicated that high efficiency of transport required domains from both the transit peptide and the mature small subunit protein.

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