Cloning, Expression and Purification of Full-Length Rep78 of Adeno-associated Virus as a Fusion Protein with Maltose Binding Protein in Escherichia coli

1995 ◽  
Vol 208 (2) ◽  
pp. 714-720 ◽  
Author(s):  
R.B. Batchu ◽  
D.A. Miles ◽  
T.M. Rechtin ◽  
R.R. Drake ◽  
P.L. Hermonat
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Full Length ◽  
Expression And Purification ◽  
Adeno Associated Virus

scholarly journals Expression of recombinant rat myo-inositol 1,4,5-trisphosphate 3-kinase B suggests a regulatory role for its N-terminus

1996 ◽  
Vol 319 (3) ◽  
pp. 713-716 ◽  
Author(s):  
Stephen THOMAS ◽  
Salvador SORIANO ◽  
Clive d'SANTOS ◽  
George BANTING
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Catalytic Domain ◽  
Maltose Binding Protein ◽  
Full Length ◽  
Regulatory Role ◽  
Calmodulin Binding ◽  
C Terminus ◽  
Inositol 1,4,5 Trisphosphate ◽  
N Terminus

We have expressed rat myo-inositol 1,4,5-trisphosphate (IP3) 3-kinase B as both a full-length, recombinant, non-fusion protein and a full-length, recombinant, fusion protein with maltose-binding protein (MBP) in Escherichia coli. The fusion protein with MBP is soluble, binds calmodulin and is enzymically active whereas the non-fusion protein is insoluble and does not bind calmodulin unless co-expressed with bacterial chaperone proteins (either GroES and GroEL, or DnaK, DnaJ and GrpE). However, soluble, calmodulin-binding non-fusion IP3 3-kinase B is enzymically inactive. The catalytic domain of the enzyme has previously been shown to reside near the C-terminus; the results we present suggest an auto-regulatory role for the N-terminus.

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